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Conflicts of interestThe authors declare no conflict of interest.REFERENCESCai Z, Penaflor C, Kuehl JV, Leebens-Mack J, et al (2006). Complete plastid genome sequences of Drimys, Liriodendron, and Piper: implications for the phylogenetic relationships of magnoliids. BMC Evol. Biol. 6: 77. http://dx.doi.org/10.1186/1471-2148-6-77 Delannoy E, Fujii S, Colas des Francs-Small C, Brundrett M, et al (2011). Rampant gene loss in the underground orchid Rhizanthella gardneri highlights evolutionary constraints on plastid genomes. Mol. Biol. Evol. 28: 2077-2086. http://dx.doi.org/10.1093/molbev/msr028 Dong W, Xu C, Cheng T, Zhou S, et al (2013). Complete chloroplast genome of Sedum sarmentosum and chloroplast genome evolution in Saxifragales. PLoS One 8: e77965. http://dx.doi.org/10.1371/journal.pone.0077965 Drew BT, Ruhfel BR, Smith SA, Moore MJ, et al (2014). Another look at the root of the angiosperms reveals a familiar tale. Syst. Biol. 63: 368-382. http://dx.doi.org/10.1093/sysbio/syt108 Frazer KA, Pachter L, Poliakov A, Rubin EM, et al (2004). VISTA: computational tools for comparative genomics. Nucleic Acids Res. 32: W273-9. http://dx.doi.org/10.1093/nar/gkh458 Goulding SE, Olmstead RG, Morden CW, Wolfe KH, et al (1996). Ebb and flow of the chloroplast inverted repeat. Mol. Gen. Genet. 252: 195-206. http://dx.doi.org/10.1007/BF02173220 Hahn C, Bachmann L, Chevreux B, et al (2013). Reconstructing mitochondrial genomes directly from genomic next-generation sequencing reads--a baiting and iterative mapping approach. Nucleic Acids Res. 41: e129. http://dx.doi.org/10.1093/nar/gkt371 Huang YY, Matzke AJM, Matzke M, et al (2013). Complete sequence and comparative analysis of the chloroplast genome of coconut palm (Cocos nucifera). PLoS One 8: e74736. http://dx.doi.org/10.1371/journal.pone.0074736 Jansen RK, Palmer JD, et al (1987). A chloroplast DNA inversion marks an ancient evolutionary split in the sunflower family (Asteraceae). Proc. Natl. Acad. Sci. USA 84: 5818-5822. http://dx.doi.org/10.1073/pnas.84.16.5818 Katti MV, Ranjekar PK, Gupta VS, et al (2001). Differential distribution of simple sequence repeats in eukaryotic genome sequences. Mol. Biol. Evol. 18: 1161-1167. http://dx.doi.org/10.1093/oxfordjournals.molbev.a003903 Kong W, Yang J, et al (2016). The complete chloroplast genome sequence of Morus mongolica and a comparative analysis within the Fabidae clade. Curr. Genet. 62: 165-172. http://dx.doi.org/10.1007/s00294-015-0507-9 Liu Y, Huo N, Dong L, Wang Y, et al (2013). Complete chloroplast genome sequences of Mongolia medicine Artemisia frigida and phylogenetic relationships with other plants. PLoS One 8: e57533. http://dx.doi.org/10.1371/journal.pone.0057533 Lohse M, Drechsel O, Bock R, et al (2007). OrganellarGenomeDRAW (OGDRAW): a tool for the easy generation of high-quality custom graphical maps of plastid and mitochondrial genomes. Curr. Genet. 52: 267-274. http://dx.doi.org/10.1007/s00294-007-0161-y Millen RS, Olmstead RG, Adams KL, Palmer JD, et al (2001). Many parallel losses of infA from chloroplast DNA during angiosperm evolution with multiple independent transfers to the nucleus. Plant Cell 13: 645-658. http://dx.doi.org/10.1105/tpc.13.3.645 Nazareno AG, Carlsen M, Lohmann LG, et al (2015). Complete chloroplast genome of Tanaecium tetragonolobum: the first Bignoniaceae plastome. PLoS One 10: e0129930. http://dx.doi.org/10.1371/journal.pone.0129930 Nock CJ, Baten A, King GJ, et al (2014). Complete chloroplast genome of Macadamia integrifolia confirms the position of the Gondwanan early-diverging eudicot family Proteaceae. BMC Genomics 15 (Suppl 9): S13. http://dx.doi.org/10.1186/1471-2164-15-S9-S13 Nguyen PA, Kim JS, Kim JH, et al (2015). The complete chloroplast genome of colchicine plants (Colchicum autumnale L. and Gloriosa superba L.) and its application for identifying the genus. Planta 242: 223-237. http://dx.doi.org/10.1007/s00425-015-2303-7 Rajendrakumar P, Biswal AK, Balachandran SM, Srinivasarao K, et al (2007). Simple sequence repeats in organellar genomes of rice: frequency and distribution in genic and intergenic regions. Bioinformatics 23: 1-4. http://dx.doi.org/10.1093/bioinformatics/btl547 Ravi V, Khurana JP, Tyagi AK, Khurana P, et al (2006). The chloroplast genome of mulberry: complete nucleotide sequence, gene organization and comparative analysis. Tree Genet. Genomes 3: 49-59. http://dx.doi.org/10.1007/s11295-006-0051-3 Ravi V, Khurana JP, Tyagi AK, Khurana P, et al (2008). An update on chloroplast genome. Plant Syst. Evol. 271: 101-122. http://dx.doi.org/10.1007/s00606-007-0608-0 Schmitz-Linneweber C, Regel R, Du TG, Hupfer H, et al (2002). The plastid chromosome of Atropa belladonna and its comparison with that of Nicotiana tabacum: the role of RNA editing in generating divergence in the process of plant speciation. Mol. Biol. Evol. 19: 1602-1612. http://dx.doi.org/10.1093/oxfordjournals.molbev.a004222 Shaw J, Lickey EB, Schilling EE, Small RL, et al (2007). Comparison of whole chloroplast genome sequences to choose noncoding regions for phylogenetic studies in angiosperms: the tortoise and the hare III. Am. J. Bot. 94: 275-288. http://dx.doi.org/10.3732/ajb.94.3.275 Steane DA, et al (2005). Complete nucleotide sequence of the chloroplast genome from the Tasmanian blue gum, Eucalyptus globulus (Myrtaceae). DNA Res. 12: 215-220. http://dx.doi.org/10.1093/dnares/dsi006 Su HJ, Hogenhout SA, Al-Sadi AM, Kuo CH, et al (2014). Complete chloroplast genome sequence of Omani lime (Citrus aurantiifolia) and comparative analysis within the rosids. PLoS One 9: e113049. http://dx.doi.org/10.1371/journal.pone.0113049 Tamura K, Stecher G, Peterson D, Filipski A, et al (2013). MEGA6: Molecular evolutionary genetics analysis version 6.0. Mol. Biol. Evol. 30: 2725-2729. http://dx.doi.org/10.1093/molbev/mst197 Walker JF, Zanis MJ, Emery NC, et al (2014). Comparative analysis of complete chloroplast genome sequence and inversion variation in Lasthenia burkei (Madieae, Asteraceae). Am. J. Bot. 101: 722-729. http://dx.doi.org/10.3732/ajb.1400049 Wu CS, Lai YT, Lin CP, Wang YN, et al (2009). Evolution of reduced and compact chloroplast genomes (cpDNAs) in gnetophytes: selection toward a lower-cost strategy. Mol. Phylogenet. Evol. 52: 115-124. http://dx.doi.org/10.1016/j.ympev.2008.12.026 Yang Z, Yoder AD, et al (1999). Estimation of the transition/transversion rate bias and species sampling. J. Mol. Evol. 48: 274-283. http://dx.doi.org/10.1007/PL00006470 Zerega NJ, Clement WL, Datwyler SL, Weiblen GD, et al (2005). Biogeography and divergence times in the mulberry family (Moraceae). Mol. Phylogenet. Evol. 37: 402-416. http://dx.doi.org/10.1016/j.ympev.2005.07.004 Zhang H, Li C, Miao H, Xiong S, et al (2013). Insights from the complete chloroplast genome into the evolution of Sesamum indicum L. PLoS One 8: e80508. http://dx.doi.org/10.1371/journal.pone.0080508 Zhang SD, Soltis DE, Yang Y, Li DZ, et al (2011). Multi-gene analysis provides a well-supported phylogeny of Rosales. Mol. Phylogenet. Evol. 60: 21-28. http://dx.doi.org/10.1016/j.ympev.2011.04.008  

Andersson L, Lunden A, Sigurdardottir S, Davies CJ, et al. (1988). Linkage relationships in the bovine MHC region. High recombination frequency between class II subregions. Immunogenetics 27: 273-280. http://dx.doi.org/10.1007/BF00376122 PMid:2894354   Ast G (2004). How did alternative splicing evolve? Nat. Rev. Genet. 5: 773-782. http://dx.doi.org/10.1038/nrg1451 PMid:15510168   Awdeh ZL and Alper CA (1980). Inherited structural polymorphism of the fourth component of human complement. Proc. Natl. Acad. Sci. U. S. A. 77: 3576-3580. http://dx.doi.org/10.1073/pnas.77.6.3576 PMid:6932037 PMCid:349660   Belt KT, Yu CY, Carroll MC and Porter RR (1985). Polymorphism of human complement component C4. Immunogenetics 21: 173-180. http://dx.doi.org/10.1007/BF00364869 PMid:3838531   Bradley A (2002). Bovine mastitis: an evolving disease. Vet. J. 164: 116-128. http://dx.doi.org/10.1053/tvjl.2002.0724 PMid:12359466   Chacko E and Ranganathan S (2009). Genome-wide analysis of alternative splicing in cow: implications in bovine as a model for human diseases. BMC Genomics 10 (Suppl 3): S11. http://dx.doi.org/10.1186/1471-2164-10-S3-S11 PMid:19958474 PMCid:2788363   Cox BJ and Robins DM (1988). Tissue-specific variation in C4 and Slp gene regulation. Nucleic Acids Res. 16: 6857-6870. http://dx.doi.org/10.1093/nar/16.14.6857 PMid:3405752 PMCid:338338   Dahl MR, Thiel S, Matsushita M, Fujita T, et al. (2001). MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway. Immunity 15: 127-135. http://dx.doi.org/10.1016/S1074-7613(01)00161-3   Dodds AW and Law SK (1990). The complement component C4 of mammals. Biochem. J. 265: 495-502. PMid:2302180 PMCid:1136911   Galante PA, Sakabe NJ, Kirschbaum-Slager N and de Souza SJ (2004). Detection and evaluation of intron retention events in the human transcriptome. RNA 10: 757-765. http://dx.doi.org/10.1261/rna.5123504 PMid:15100430 PMCid:1370565   Garcia-Blanco MA, Baraniak AP and Lasda EL (2004). Alternative splicing in disease and therapy. Nat. Biotechnol. 22: 535-546. http://dx.doi.org/10.1038/nbt964 PMid:15122293   Giles CM (1984). A new genetic variant for Chido. Vox Sang. 46: 149-156. http://dx.doi.org/10.1111/j.1423-0410.1984.tb00067.x PMid:6710967   Guerra-Junior G, Grumach AS, de Lemos-Marini SH, Kirschfink M, et al. (2008). Complement 4 phenotypes and genotypes in Brazilian patients with classical 21-hydroxylase deficiency. Clin. Exp. Immunol. 155: 182-188. http://dx.doi.org/10.1111/j.1365-2249.2008.03838.x PMid:19137635 PMCid:2675248   Günther J, Koczan D, Yang W, Nurnberg G, et al. (2009). Assessment of the immune capacity of mammary epithelial cells: comparison with mammary tissue after challenge with Escherichia coli. Vet. Res. 40: 31. http://dx.doi.org/10.1051/vetres/2009014 PMid:19321125 PMCid:2695127   Hull J, Campino S, Rowlands K, Chan MS, et al. (2007). Identification of common genetic variation that modulates alternative splicing. PLoS Genet. 3: e99. http://dx.doi.org/10.1371/journal.pgen.0030099 PMid:17571926 PMCid:1904363   Ju Z, Wang C, Li Q, Hou M, et al. (2011). Alternative splicing and mRNA expression analysis of bovine SLAMF7 gene in healthy and mastitis mammary tissues. Mol. Biol. Rep. DOI: 10.1007/s11033-011-1198-z. http://dx.doi.org/10.1007/s11033-011-1198-z   Keren H, Lev-Maor G and Ast G (2010). Alternative splicing and evolution: diversification, exon definition and function. Nat. Rev. Genet. 11: 345-355. http://dx.doi.org/10.1038/nrg2776 PMid:20376054   Kim E, Magen A and Ast G (2007). Different levels of alternative splicing among eukaryotes. Nucleic Acids Res. 35: 125-131. http://dx.doi.org/10.1093/nar/gkl924 PMid:17158149 PMCid:1802581   Larionov A, Krause A and Miller W (2005). A standard curve based method for relative real time PCR data processing. BMC Bioinformatics 6: 62. http://dx.doi.org/10.1186/1471-2105-6-62 PMid:15780134 PMCid:1274258   Le Hir H, Charlet-Berguerand N, de Franciscis V and Thermes C (2002). 5'-End RET splicing: absence of variants in normal tissues and intron retention in pheochromocytomas. Oncology 63: 84-91. http://dx.doi.org/10.1159/000065725 PMid:12187076   Liu HX, Cartegni L, Zhang MQ and Krainer AR (2001). A mechanism for exon skipping caused by nonsense or missense mutations in BRCA1 and other genes. Nat. Genet. 27: 55-58. http://dx.doi.org/10.1038/83762 PMid:11137998   Morera AL, Henry M, Garcia-Hernandez A and Fernandez-Lopez L (2007). Acute phase proteins as biological markers of negative psychopathology in paranoid schizophrenia. Actas Esp. Psiquiatr. 35: 249-252. PMid:17592787   Pattanakitsakul S, Zheng JH, Natsuume-Sakai S, Takahashi M, et al. (1992). Aberrant splicing caused by the insertion of the B2 sequence into an intron of the complement C4 gene is the basis for low C4 production in H-2k mice. J. Biol. Chem. 267: 7814-7820. PMid:1373139   Petri M, Watson R, Winkelstein JA and McLean RH (1993). Clinical expression of systemic lupus erythematosus in patients with C4A deficiency. Medicine 72: 236-244. http://dx.doi.org/10.1097/00005792-199307000-00003 PMid:8341140   Rainard P and Poutrel B (1995). Deposition of complement components on Streptococcus agalactiae in bovine milk in the absence of inflammation. Infect. Immun. 63: 3422-3427. PMid:7642272 PMCid:173471   Rio DC (1991). Regulation of Drosophila P element transposition. Trends Genet. 7: 282-287. PMid:1662417   Rupp R and Boichard D (2003). Genetics of resistance to mastitis in dairy cattle. Vet. Res. 34: 671-688. http://dx.doi.org/10.1051/vetres:2003020 PMid:14556700   Vergani D, Johnston C, Abdullah N and Barnett AH (1983). Low serum C4 concentrations: an inherited predisposition to insulin dependent diabetes? Br. Med. J. 286: 926-928. http://dx.doi.org/10.1136/bmj.286.6369.926   Wang Z, Zhang S and Wang G (2008). Response of complement expression to challenge with lipopolysaccharide in embryos/larvae of zebrafish Danio rerio: acquisition of immunocompetent complement. Fish Shellfish Immunol. 25: 264-270. http://dx.doi.org/10.1016/j.fsi.2008.05.010 PMid:18657447   Witte DP, Welch TR and Beischel LS (1991). Detection and cellular localization of human C4 gene expression in the renal tubular epithelial cells and other extrahepatic epithelial sources. Am. J. Pathol. 139: 717-724. PMid:1928296 PMCid:1886325   Yang Y, Chung EK, Zhou B, Blanchong CA, et al. (2003). Diversity in intrinsic strengths of the human complement system: serum C4 protein concentrations correlate with C4 gene size and polygenic variations, hemolytic activities, and body mass index. J. Immunol. 171: 2734-2745. PMid:12928427   Yu CY, Belt KT, Giles CM, Campbell RD, et al. (1986). Structural basis of the polymorphism of human complement components C4A and C4B: gene size, reactivity and antigenicity. EMBO J. 5: 2873-2881. PMid:2431902 PMCid:1167237

Agah A, Montalto MC, Young K and Stahl GL (2001). Isolation, cloning and functional characterization of porcine mannose-binding lectin. Immunology 102: 338-343. http://dx.doi.org/10.1046/j.1365-2567.2001.01191.x PMid:11298833 PMCid:1783182   Arora M, Munoz E and Tenner AJ (2001). Identification of a site on mannan-binding lectin critical for enhancement of phagocytosis. J. Biol. Chem. 276: 43087-43094. http://dx.doi.org/10.1074/jbc.M105455200 PMid:11533031   Brown-Augsburger P, Hartshorn K, Chang D, Rust K, et al. (1996). Site-directed mutagenesis of Cys-15 and Cys-20 of pulmonary surfactant protein D. Expression of a trimeric protein with altered anti-viral properties. J. Biol. Chem. 271: 13724-13730. http://dx.doi.org/10.1074/jbc.271.23.13724 PMid:8662732   Capparelli R, Parlato M, Amoroso MG, Roperto S, et al. (2008). Mannose-binding lectin haplotypes influence Brucella abortus infection in the water buffalo (Bubalus bubalis). Immunogenetics 60: 157-165. http://dx.doi.org/10.1007/s00251-008-0284-4 PMid:18330558   Chaneton L, Tirante L, Maito J, Chaves J, et al. (2008). Relationship between milk lactoferrin and etiological agent in the mastitic bovine mammary gland. J. Dairy Sci. 91: 1865-1873. http://dx.doi.org/10.3168/jds.2007-0732 PMid:18420617   Eisen DP and Minchinton RM (2003). Impact of mannose-binding lectin on susceptibility to infectious diseases. Clin. Infect. Dis. 37: 1496-1505. http://dx.doi.org/10.1086/379324 PMid:14614673   Fallin D, Cohen A, Essioux L, Chumakov I, et al. (2001). Genetic analysis of case/control data using estimated haplotype frequencies: application to APOE locus variation and Alzheimer's disease. Genome Res. 11: 143-151. http://dx.doi.org/10.1101/gr.148401 PMid:11156623 PMCid:311030   Gjerstorff M, Hansen S, Jensen B, Dueholm B, et al. (2004). The genes encoding bovine SP-A, SP-D, MBL-A, conglutinin, CL-43 and CL-46 form a distinct collectin locus on Bos taurus chromosome 28 (BTA28) at position q.1.8-1.9. Anim. Genet. 35: 333-337. http://dx.doi.org/10.1111/j.1365-2052.2004.01167.x PMid:15265076   Holmskov U, Thiel S and Jensenius JC (2003). Collections and ficolins: humoral lectins of the innate immune defense. Annu. Rev. Immunol. 21: 547-578. http://dx.doi.org/10.1146/annurev.immunol.21.120601.140954 PMid:12524383   Huang J, Wang H, Wang C, Li J, et al. (2010). Single nucleotide polymorphisms, haplotypes and combined genotypes of lactoferrin gene and their associations with mastitis in Chinese Holstein cattle. Mol. Biol. Rep. 37: 477-483. http://dx.doi.org/10.1007/s11033-009-9669-1 PMid:19672694   Jensen PH, Weilguny D, Matthiesen F, McGuire KA, et al. (2005). Characterization of the oligomer structure of recombinant human mannan-binding lectin. J. Biol. Chem. 280: 11043-11051. http://dx.doi.org/10.1074/jbc.M412472200 PMid:15653690   Kawai T, Suzuki Y, Eda S, Ohtani K, et al. (1997). Cloning and characterization of a cDNA encoding bovine mannan-binding protein. Gene 186: 161-165. http://dx.doi.org/10.1016/S0378-1119(96)00664-6   Kawasaki N, Kawasaki T and Yamashina I (1983). Isolation and characterization of a mannan-binding protein from human serum. J. Biochem. 94: 937-947. PMid:6643429   Larsen F, Madsen HO, Sim RB, Koch C, et al. (2004). Disease-associated mutations in human mannose-binding lectin compromise oligomerization and activity of the final protein. J. Biol. Chem. 279: 21302-21311. http://dx.doi.org/10.1074/jbc.M400520200 PMid:14764589   Lillie BN, Brooks AS, Keirstead ND and Hayes MA (2005). Comparative genetics and innate immune functions of collagenous lectins in animals. Vet. Immunol. Immunopathol. 108: 97-110. http://dx.doi.org/10.1016/j.vetimm.2005.07.001 PMid:16098608   Lillie BN, Keirstead ND, Squires EJ and Hayes MA (2006). Single-nucleotide polymorphisms in porcine mannan-binding lectin A. Immunogenetics 58: 983-993. http://dx.doi.org/10.1007/s00251-006-0160-z PMid:17089118   Lillie BN, Keirstead ND, Squires EJ and Hayes MA (2007). Gene polymorphisms associated with reduced hepatic expression of porcine mannan-binding lectin C. Dev. Comp. Immunol. 31: 830-846. http://dx.doi.org/10.1016/j.dci.2006.11.002 PMid:17194476   Ma BY, Nakamura N, Dlabac V, Naito H, et al. (2007). Isolation, cloning, and characterization of a novel phosphomannan-binding lectin from porcine serum. J. Biol. Chem. 282: 12963-12975. http://dx.doi.org/10.1074/jbc.M611820200 PMid:17324926   Madsen HO, Garred P, Kurtzhals JA, Lamm LU, et al. (1994). A new frequent allele is the missing link in the structural polymorphism of the human mannan-binding protein. Immunogenetics 40: 37-44. http://dx.doi.org/10.1007/BF00163962 PMid:8206524   Madsen HO, Satz ML, Hogh B, Svejgaard A, et al. (1998). Different molecular events result in low protein levels of mannan-binding lectin in populations from southeast Africa and South America. J. Immunol. 161: 3169-3175. PMid:9743385   Nepomuceno RR, Henschen-Edman AH, Burgess WH and Tenner AJ (1997). cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro. Immunity 6: 119-129. http://dx.doi.org/10.1016/S1074-7613(00)80419-7   Neth O, Jack DL, Dodds AW, Holzel H, et al. (2000). Mannose-binding lectin binds to a range of clinically relevant microorganisms and promotes complement deposition. Infect. Immun. 68: 688-693. http://dx.doi.org/10.1128/IAI.68.2.688-693.2000 PMid:10639434 PMCid:97193   Ohashi T and Erickson HP (2004). The disulfide bonding pattern in ficolin multimers. J. Biol. Chem. 279: 6534-6539. http://dx.doi.org/10.1074/jbc.M310555200 PMid:14660572   Podolsky MJ, Lasker A, Flaminio MJ, Gowda LD, et al. (2006). Characterization of an equine mannose-binding lectin and its roles in disease. Biochem. Biophys. Res. Commun. 343: 928-936. http://dx.doi.org/10.1016/j.bbrc.2006.03.055 PMid:16574074   Qiu H (2002). Modern Dairy Science. Agriculture Press, China, 1-12.   Risch NJ (2000). Searching for genetic determinants in the new millennium. Nature 405: 847-856. http://dx.doi.org/10.1038/35015718 PMid:10866211   Rupp R and Boichard D (1999). Genetic parameters for clinical mastitis, somatic cell score, production, udder type traits, and milking ease in first lactation Holsteins. J. Dairy Sci. 82: 2198-2204. http://dx.doi.org/10.3168/jds.S0022-0302(99)75465-2   Seegers H, Fourichon C and Beaudeau F (2003). Production effects related to mastitis and mastitis economics in dairy cattle herds. Vet. Res. 34: 475-491. http://dx.doi.org/10.1051/vetres:2003027 PMid:14556691   Shi L, Takahashi K, Dundee J, Shahroor-Karni S, et al. (2004). Mannose-binding lectin-deficient mice are susceptible to infection with Staphylococcus aureus. J. Exp. Med. 199: 1379-1390. http://dx.doi.org/10.1084/jem.20032207 PMid:15148336 PMCid:2211809   Shi YY and He L (2005). SHEsis, a powerful software platform for analyses of linkage disequilibrium, haplotype construction, and genetic association at polymorphism loci. Cell Res. 15: 97-98. http://dx.doi.org/10.1038/sj.cr.7290272 PMid:15740637   Smithson A, Munoz A, Suarez B, Soto SM, et al. (2007). Association between mannose-binding lectin deficiency and septic shock following acute pyelonephritis due to Escherichia coli. Clin. Vaccine Immunol. 14: 256-261. http://dx.doi.org/10.1128/CVI.00400-06 PMid:17202308 PMCid:1828851   Takahashi R, Tsutsumi A, Ohtani K, Muraki Y, et al. (2005). Association of mannose binding lectin (MBL) gene polymorphism and serum MBL concentration with characteristics and progression of systemic lupus erythematosus. Ann. Rheum. Dis. 64: 311-314. http://dx.doi.org/10.1136/ard.2003.020172 PMid:15647440 PMCid:1755352   Wakamiya N, Okuno Y, Sasao F, Ueda S, et al. (1992). Isolation and characterization of conglutinin as an influenza A virus inhibitor. Biochem. Biophys. Res. Commun. 187: 1270-1278. http://dx.doi.org/10.1016/0006-291X(92)90440-V   Wallis R, Shaw JM, Uitdehaag J, Chen CB, et al. (2004). Localization of the serine protease-binding sites in the collagen-like domain of mannose-binding protein: indirect effects of naturally occurring mutations on protease binding and activation. J. Biol. Chem. 279: 14065-14073. http://dx.doi.org/10.1074/jbc.M400171200 PMid:14724269

Ardehali R, Shi L, Janatova J, Mohammad SF, et al. (2003). The inhibitory activity of serum to prevent bacterial adhesion is mainly due to apo-transferrin. J. Biomed. Mater. Res. A 66: 21-28. http://dx.doi.org/10.1002/jbm.a.10493 PMid:12833427   Ashton GC, Fallon GR and Suthcrland DN (1964). Transferrin (β-globulin) type and milk and butterfat production in dairy cows. J. Agric. Sci. 62: 27-34. http://dx.doi.org/10.1017/S0021859600059736   Bashirullah A, Cooperstock RL and Lipshitz HD (2001). Spatial and temporal control of RNA stability. Proc. Natl. Acad. Sci. U. S. A. 98: 7025-7028. http://dx.doi.org/10.1073/pnas.111145698 PMid:11416182 PMCid:34617   Beckman L and Beckman G (1986). Transferrin C2 as an enhancer of cyto- and genotoxic damage. Prog. Clin. Biol. Res. 209B: 221-224. PMid:3749080   Bond R, Kim JY and Lloyd DH (2005). Bovine and canine transferrin inhibit the growth of Malassezia pachydermatis in vitro. Med. Mycol. 43: 447-451. http://dx.doi.org/10.1080/13693780400020154 PMid:16178374   Brandon RB, Giffard JM and Bell K (1999). Single nucleotide polymorphisms in the equine transferrin gene. Anim. Genet. 30: 439-443. http://dx.doi.org/10.1046/j.1365-2052.1999.00546.x PMid:10612233   Casas E, Keele JW, Shackelford SD, Koohmaraie M, et al. (2004). Identification of quantitative trait loci for growth and carcass composition in cattle. Anim. Genet. 35: 2-6. http://dx.doi.org/10.1046/j.1365-2052.2003.01067.x PMid:14731222   Chaneton L, Tirante L, Maito J, Chaves J, et al. (2008). Relationship between milk lactoferrin and etiological agent in the mastitic bovine mammary gland. J. Dairy Sci. 91: 1865-1873. http://dx.doi.org/10.3168/jds.2007-0732 PMid:18420617   Chowdhary BP, Raudsepp T, Fronicke L and Scherthan H (1998). Emerging patterns of comparative genome organization in some mammalian species as revealed by Zoo-FISH. Genome Res. 8: 577-589. PMid:9647633   Douabin-Gicquel V, Soriano N, Ferran H, Wojcik F, et al. (2001). Identification of 96 single nucleotide polymorphisms in eight genes involved in iron metabolism: efficiency of bioinformatic extraction compared with a systematic sequencing approach. Hum. Genet. 109: 393-401. http://dx.doi.org/10.1007/s004390100599 PMid:11702220   Enns CA and Sussman HH (1981). Physical characterization of the transferrin receptor in human placentae. J. Biol. Chem. 256: 9820-9823. PMid:6268632   Fallin D, Cohen A, Essioux L, Chumakov I, et al. (2001). Genetic analysis of case/control data using estimated haplotype frequencies: application to APOE locus variation and Alzheimer's disease. Genome Res. 11: 143-151. http://dx.doi.org/10.1101/gr.148401 PMid:11156623 PMCid:311030   Fletcher J and Huehns ER (1968). Function of transferrin. Nature 218: 1211-1214. http://dx.doi.org/10.1038/2181211a0 PMid:5656647   Gahne B, Juneja RK and Grolmus J (1977). Horizontal polyacrylamide gradient gel electrophoresis for the simultaneous phenotyping of transferrin, post-transferrin, albumin and post-albumin in the blood plasma of cattle. Anim. Blood Groups Biochem. Genet. 8: 127-137. http://dx.doi.org/10.1111/j.1365-2052.1977.tb01637.x PMid:603096   Heringstad B, Klemetsdal G and Ruane J (2000). Selection for mastitis resistance in dairy cattle: a review with focus on the situation in the Nordic countries. Livest. Prod. Sci. 64: 95-106. http://dx.doi.org/10.1016/S0301-6226(99)00128-1   Huang J, Wang H, Wang C, Li J, et al. (2010). Single nucleotide polymorphisms, haplotypes and combined genotypes of lactoferrin gene and their associations with mastitis in Chinese Holstein cattle. Mol. Biol. Rep. 37: 477-483. http://dx.doi.org/10.1007/s11033-009-9669-1 PMid:19672694   Jansen RP (2001). mRNA localization: message on the move. Nat. Rev. Mol. Cell. Biol. 2: 247-256. http://dx.doi.org/10.1038/35067016 PMid:11283722   Kappes SM, Keele JW, Stone RT, McGraw RA, et al. (1997). A second-generation linkage map of the bovine genome. Genome Res. 7: 235-249. http://dx.doi.org/10.1101/gr.7.3.235 PMid:9074927   Khatib H, Zaitoun I, Chang YM, Maltecca C, et al. (2007). Evaluation of association between polymorphism within the thyroglobulin gene and milk production traits in dairy cattle. J. Anim. Breed. Genet. 124: 26-28. http://dx.doi.org/10.1111/j.1439-0388.2007.00634.x PMid:17302957   Kmiec M (1998). Transferyna- bia ko pe niace wiele ról w organizmie. Przegl. Hodowlany 1: 8-9.   Kruglyak L (1999). Prospects for whole-genome linkage disequilibrium mapping of common disease genes. Nat. Genet. 22: 139-144. http://dx.doi.org/10.1038/9642 PMid:10369254   Lambert LA, Perri H, Halbrooks PJ and Mason AB (2005). Evolution of the transferrin family: conservation of residues associated with iron and anion binding. Comp. Biochem. Physiol. B. Biochem. Mol. Biol. 142: 129-141. http://dx.doi.org/10.1016/j.cbpb.2005.07.007 PMid:16111909   Larionov A, Krause A and Miller W (2005). A standard curve based method for relative real time PCR data processing. BMC Bioinformatics 6: 62. http://dx.doi.org/10.1186/1471-2105-6-62 PMid:15780134 PMCid:1274258   Liu W, Wang J, Li Q, Ju Z, et al. (2010). Correlation analysis between three novel SNPs of the Src gene in bovine and milk production traits. Mol. Biol. Rep. 37: 3771-3777. http://dx.doi.org/10.1007/s11033-010-0031-4 PMid:20213510   MacGillivray RT, Mendez E, Sinha SK, Sutton MR, et al. (1982). The complete amino acid sequence of human serum transferrin. Proc. Natl. Acad. Sci. U. S. A. 79: 2504-2508. http://dx.doi.org/10.1073/pnas.79.8.2504 PMid:6953407 PMCid:346227   Majewski J and Ott J (2002). Distribution and characterization of regulatory elements in the human genome. Genome Res. 12: 1827-1836. http://dx.doi.org/10.1101/gr.606402 PMid:12466286 PMCid:187578   Mason C (2006). Basic mastitis bacteriology: untangling the pathogens. Ir. Vet. J. 59: 453-459.   Nott A, Meislin SH and Moore MJ (2003). A quantitative analysis of intron effects on mammalian gene expression. RNA 9: 607-617. http://dx.doi.org/10.1261/rna.5250403 PMid:12702819 PMCid:1370426   Poso J and Mantysaari EA (1996). Relationships between clinical mastitis, somatic cell score, and production for the first three lactations of Finnish Ayrshire. J. Dairy Sci. 79: 1284-1291. http://dx.doi.org/10.3168/jds.S0022-0302(96)76483-4   Retzer MD, Kabani A, Button LL, Yu RH, et al. (1996). Production and characterization of chimeric transferrins for the determination of the binding domains for bacterial transferrin receptors. J. Biol. Chem. 271: 1166-1173. http://dx.doi.org/10.1074/jbc.271.2.1166 PMid:8557646   Rupp R and Boichard D (1999). Genetic parameters for clinical mastitis, somatic cell score, production, udder type traits, and milking ease in first lactation Holsteins. J. Dairy Sci. 82: 2198-2204. http://dx.doi.org/10.3168/jds.S0022-0302(99)75465-2   Sanz A, Ordovas L, Serrano C, Zaragoza P, et al. (2010). A single nucleotide polymorphism in the coding region of bovine transferrin is associated with milk fat yield. Genet. Mol. Res. 9: 843-848. http://dx.doi.org/10.4238/vol9-2gmr784 PMid:20449817   Seegers H, Fourichon C and Beaudeau F (2003). Production effects related to mastitis and mastitis economics in dairy cattle herds. Vet. Res. 34: 475-491. http://dx.doi.org/10.1051/vetres:2003027 PMid:14556691   Sevi A, Taibi L, Albenzio M, Annicchiarico G, et al. (2001). Airspace effects on the yield and quality of ewe milk. J. Dairy Sci. 84: 2632-2640. http://dx.doi.org/10.3168/jds.S0022-0302(01)74717-0   Shi YY and He L (2005). SHEsis, a powerful software platform for analyses of linkage disequilibrium, haplotype construction, and genetic association at polymorphism loci. Cell Res. 15: 97-98. http://dx.doi.org/10.1038/sj.cr.7290272 PMid:15740637   Steppa R, Wójtowskl J, Bielinska S and Keszycka M (2009). Effect of transferrin and haemoglobin polymorphism on hygienic quality of milk in sheep. Züchtungskunde 81: 125-132.   Swanson KM, Stelwagen K, Dobson J, Henderson HV, et al. (2009). Transcriptome profiling of Streptococcus uberis-induced mastitis reveals fundamental differences between immune gene expression in the mammary gland and in a primary cell culture model. J. Dairy Sci. 92: 117-129. http://dx.doi.org/10.3168/jds.2008-1382 PMid:19109270   Tao Q, Yu MX, Zhao YH and Wang DX (2007). Survey of incidence of cow mastitis in west Liaoning and the integrated control measures. China Cattle Sci. 4: 61-63 (in Chinese).   Wedekind C (1994). Mate choice and maternal selection for specific parasite resistances before; during and after fertilization. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 346: 303-311. http://dx.doi.org/10.1098/rstb.1994.0147 PMid:7708826   Zhang F, Huang J, Li Q, Ju Z, et al. (2010). Novel single nucleotide polymorphisms (SNPs) of the bovine STAT4 gene and their associations with production traits in Chinese Holstein cattle. Afr. J. Biotechnol. 9: 4003-4008.   Zhang YH, Pan YS, Gao Y, Ma Q, et al. (2008). Studies on transferrin and posttremsferr polymorphism and their relationship with performances in red steppe. Agric. Sci. Technol. 9: 109-112.

Baker EN and Baker HM (2005). Molecular structure, binding properties and dynamics of lactoferrin. Cell Mol. Life Sci. 62: 2531-2539. http://dx.doi.org/10.1007/s00018-005-5368-9 PMid:16261257 Bannerman DD, Paape MJ, Lee JW, Zhao X, et al. (2004). Escherichia coli and Staphylococcus aureus elicit differential innate immune responses following intramammary infection. Clin. Diagn. Lab. Immunol. 11: 463-472. PMid:15138171    PMCid:404560 Chaneton L, Tirante L, Maito J, Chaves J, et al. (2008). Relationship between milk lactoferrin and etiological agent in the mastitic bovine mammary gland. J. Dairy Sci. 91: 1865-1873. http://dx.doi.org/10.3168/jds.2007-0732 PMid:18420617 Garcia-Blanco MA, Baraniak AP and Lasda EL (2004). Alternative splicing in disease and therapy. Nat. Biotechnol. 22: 535-546. http://dx.doi.org/10.1038/nbt964 PMid:15122293 Hagiwara S, Kawai K, Anri A and Nagahata H (2003). Lactoferrin concentrations in milk from normal and subclinical mastitic cows. J. Vet. Med. Sci. 65: 319-323. http://dx.doi.org/10.1292/jvms.65.319 PMid:12679560 Huang JM, Wang HM, Wang CF, Li JB, et al. (2010). Single nucleotide polymorphisms, haplotypes and combined genotypes of lactoferrin gene and their associations with mastitis in Chinese Holstein cattle. Mol. Bio. Rep. 37: 477- 483. http://dx.doi.org/10.1007/s11033-009-9669-1 PMid:19672694 Hurley WL and Rejman JJ (1993). Bovine lactoferrin in involuting mammary tissue. Cell Biol. Int. 17: 283-289. http://dx.doi.org/10.1006/cbir.1993.1064 PMid:8513296 Kawai K, Hagiwara S, Anri A and Nagahata H (1999). Lactoferrin concentration in milk of bovine clinical mastitis. Vet. Res. Commun. 23: 391-398. http://dx.doi.org/10.1023/A:1006347423426 PMid:10598071 Komine K, Komine Y, Kuroishi T, Kobayashi J, et al. (2005). Small molecule lactoferrin with an inflammatory effect but no apparent antibacterial activity in mastitic mammary gland secretion. J. Vet. Med. Sci 67: 667-677. http://dx.doi.org/10.1292/jvms.67.667 PMid:16082114 Larionov A, Krause A and Miller W (2005). A standard curve based method for relative real time PCR data processing. BMC Bioinformatics 6: 62. http://dx.doi.org/10.1186/1471-2105-6-62 PMid:15780134    PMCid:1274258 Lynch KW (2004). Consequences of regulated pre-mRNA splicing in the immune system. Nat. Rev. Immunol. 4: 931-940. http://dx.doi.org/10.1038/nri1497 PMid:15573128 Nagahata H, Ito H, Maruta H, Nishikawa Y, et al. (2007). Controlling highly prevalent Staphylococcus aureus mastitis from the dairy farm. J. Vet. Med. Sci. 69: 893-898. http://dx.doi.org/10.1292/jvms.69.893 PMid:17917373 Nickerson SC, Owens WE and Boddie RL (1995). Mastitis in dairy heifers: initial studies on prevalence and control. J. Dairy Sci. 78: 1607-1618. http://dx.doi.org/10.3168/jds.S0022-0302(95)76785-6 Pawlik A, Sender G and Korwin-Kossakowska A (2009). Bovine lactoferrin gene polymorphism and expression in relation to mastitis resistance-a review. Anim. Sci. Pap. Rep. 27: 263-271. Pitkala A, Haveri M, Pyorala S, Myllys V, et al. (2004). Bovine mastitis in Finland 2001 - prevalence, distribution of bacteria, and antimicrobial resistance. J. Dairy Sci. 87: 2433-2441. http://dx.doi.org/10.3168/jds.S0022-0302(04)73366-4 Stamm S, Ben-Ari S, Rafalska I, Tang Y, et al. (2005). Function of alternative splicing. Gene 344: 1-20. http://dx.doi.org/10.1016/j.gene.2004.10.022 PMid:15656968 Swanson KM, Stelwagen K, Dobson J, Henderson HV, et al. (2009). Transcriptome profiling of Streptococcus uberis-induced mastitis reveals fundamental differences between immune gene expression in the mammary gland and in a primary cell culture model. J. Dairy Sci. 92: 117-129. http://dx.doi.org/10.3168/jds.2008-1382 PMid:19109270 Ward PP, Paz E and Conneely OM (2005). Multifunctional roles of lactoferrin: a critical overview. Cell Mol. Life Sci. 62: 2540-2548. http://dx.doi.org/10.1007/s00018-005-5369-8 PMid:16261256 Wellnitz O and Kerr DE (2004). Cryopreserved bovine mammary cells to model epithelial response to infection. Vet. Immunol. Immunopathol. 101: 191-202. http://dx.doi.org/10.1016/j.vetimm.2004.04.019 PMid:15350749