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Kalashnikova L.A., Murugina N.E., Bagal I.E., Kalashnikov A.E., Kalashnikov V.E. The role of pattern-recognizing receptors of innate immunity cells in the pathogenesis of cattle diseases (review). Sel'skokhozyaistvennaya Biologiya [Agricultural Biology], 2025,Vol. 60, № 2, p. 183-198.
(how to cite this article)

doi: 10.15389/agrobiology.2025.2.183eng

UDC: 636.2.034:636.082.2

Acknowledgements:
Supported by a grant from the Russian Science Foundation (project No. 23-26-00235)

 

THE ROLE OF PATTERN-RECOGNIZING RECEPTORS OF INNATE IMMUNITY CELLS IN THE PATHOGENESIS OF CATTLE DISEASES (review)

L.A. Kalashnikova1✉, N.E. Murugina2, I.E. Bagal1,
A.E. Kalashnikov1, V.E. Kalashnikov1

1All Russian Research Institute of Animal Breeding, 13, ul. Lenina, pos. Lesnye Polyany, Pushkino city district, Moscow Province, 141212 Russia, e-mail lakalashnikova@mail.ru (✉ corresponding author), ade_57@mail.ru,
aekalashnikov@yandex.ru, vekalashnikov@yandex.ru;

2National Research Center Institute of Immunology, 24, Kashirskoe sh., Moscow, 115522 Russia, e-mail
nemurugina@yandex.ru

ORCID:
Kalashnikova L.A. orcid.org/0000-0002-9760-5254
Kalashnikov A.E. orcid.org/0000-0003-1600-7357
Murugina N.E. orcid.org/0000-0001-7000-5729
Kalashnikov V.E. orcid.org/0009-0009-4259-1957
Bagal I.E. orcid.org/0009-0000-9365-0544

Final revision received July 31, 2024
Accepted September 17, 2024

The problem of increasing the natural resistance of highly productive cattle environment in industrial conditions is becoming increasingly relevant. Infections of the mammary glands, reproductive system, and viral diseases of cattle entail economic spends associated with a decrease in milk production, treatment costs and culling of weak animals. The key to maintaining homeostasis in the body and preserving the health of the animal is the timely recognition of pathogens by cells of the innate immune system. Currently, many molecular mechanisms of the immune cell activation have been established by human and mouse models; the role of pattern recognition receptors (PRRs) (J. Xu et al., 2011; I.F. Moretti et al., 2018), adapter proteins and transcription factors in the formation of an immune response has been shown (T. Kawai et al., 2008), which includes not only the recognition and removal of foreign pathogens, but and elimination of damaged cells of one’s own body (O. Takeuchi et al., 2010; N. Kano et al., 2022). This review present modern data on the role of PRRs in recognizing pathogens and activating cells of the innate immune system in cattle: the main immunogenic structures (PAMPs and DAMPs) that affect the cells of the innate immune system in cattle are described, information on the structure and functions of the main groups of PRRs is collected , including Toll-like (TLR), NOD-like (NLR), C-type lectin-like receptors (CLR) and RIG1-like (RLR) receptors, the structural features of these receptors in cattle are shown (Z. Sladek et al., 2009; S.K. Mishra et al., 2019). In cattle, 10 functional TLRs (TLR1 to TLR10) have been identified and mapped, each recognizing specific molecular patterns associated with pathogens (M. Maurić Maljković et al., 2023), 32 types of CLR molecules, most of which can be identified as orthologs of human and mouse proteins (A. Holder et al., 2023). The NOD-like receptor family consists of 4 subfamilies. NOD1 and NOD2 play an autoregulatory role (N. Inohara et al., 1999) and are involved in signal transduction to adaptor proteins (G. Magnuson et al., 2010). RLRs include three receptors: RIG-I, MDA5 and LGP2 (K. Wicherska-Pawłowska et al., 2021), RIG-I-like receptors are cytoplasmic nucleic acid receptors for virion RNA. Their role in the induction of the innate immune response during protection against rotavirus infecti on (P.S. Paul et al., 1993; K. de Verdier Klingenberg et al., 1998) and recognition of bovine diarrhea virus has been established (Y. Ma et al., 2022).To better understand the role of PRRs in cell activation, the pathways of intracellular signal transmission from receptors upon their activation are depicted (J. Napetschnig et al., 2013; T. Kawai et al., 2008). The importance of PRR in the formation of inflammatory diseases in cattle has been shown (M. Maurić Maljković et al., 2023). Special attention is paid to the influence of PRR gene polymorphism on cattle resistance to infectious diseases such as mastitis (A.Q. de Mesquita et al., 2012), tuberculosis (A. Bhaladhare et al., 2016), paratuberculosis (R. Mucha et al., 2009; J.B. Okuni et al., 2021) and other diseases (M. Bjelka et al., 2020). Identification of PRR single nucleotide polymorphisms opens up promising opportunities for marker-based selection strategies, disease risk screening and increasing the genetic resistance of dairy cattle to diseases (M. Maurić Maljković et al., 2023).

Keywords: Pattern recognition receptors, innate immunity, PAMP, DAMP, TLR, NOD, RIG, CLR, cattle, bacterial infections, viral infections, polymorphism.

 

 

REFERENCES

  1. Takeuchi O., Akira S. Pattern recognition receptors and inflammation. Cell, 2010, 140(6): 805-820 CrossRef
  2. Phongsisay V. The immunobiology of Campylobacter jejuni: Innate immunity and autoimmune diseases. Immunobiology, 2016, 221(4): 535-543 CrossRef
  3. Janeway C.A. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb. Symp. Quant. Biol., 1989, 54: 1-13 CrossRef
  4. Janeway Jr. C.A., Medzhitov R. Innate immune recognition. Annual Review of Immunology,2002, 20: 197-216 CrossRef
  5. Zhang Q., Raoof M., Chen Y., Sumi Y., Sursal T., Junger W., Brohi K., Itagaki K., Hauser C.J. Circulating mitochondrial DAMPs cause inflammatory responses to injury. Nature, 2010, 464(7285): 104-107 CrossRef
  6. Xu J., Zhang X., Monestier M., Esmon N.L., Esmon C.T. Extracellular histones are mediators of death through TLR2 and TLR4 in mouse fatal liver injury. J. Immunol., 2011, 187(5): 2626-263 CrossRef
  7. Kano N., Ong G.H., Ori D., Kawai T. Pathophysiological role of nucleic acid-sensing pattern recognition receptors in inflammatory diseases. Front. Cell. Infect. Microbiol., 2022, 12: 910654 CrossRef
  8. Ohashi K., Burkart V., Flohé S., Kolb H. Cutting edge: heat shock protein 60 is a putative endogenous ligand of the toll-like receptor-4 complex. J. Immunol., 2000, 164(2): 558-561 CrossRef
  9. Yang H., Wang H., Andersson U. Targeting inflammation driven by HMGB1. Front. Immunol., 2020, 11: 484 CrossRef
  10. Powell J.D., Horton M.R. Threat matrix: low-molecular-weight hyaluronan (HA) as a danger signal. Immunol. Res., 2005, 31(3): 207-218 CrossRef
  11. Roh J.S., Sohn D.H. Damage-associated molecular patterns in inflammatory diseases. Immune Netw., 2018, 18(4): e27 CrossRef
  12. Murao A., Aziz M., Wang H., Brenner M., Wang P. Release mechanisms of major DAMPs. Apoptosis, 2021, 26(3-4): 152-162 CrossRef
  13. Russo A.J., Vasudevan S.O., Méndez-Huergo S.P., Kumari P., Menoret A., Duduskar S.. Wang C., Pérez Sáez J.M., Fettis M.M., Li C., Liu R., Wanchoo A., Chandiran K., Ruan J., Vanaja S.K., Bauer M., Sponholz C., Hudalla G.A., Vella A.T., Zhou B., Deshmukh S.D., Rabinovich G.A., Rathinam V.A. Intracellular immune sensing promotes inflammation via gasdermin D-driven release of a lectin alarmin. Nat. Immunol., 2021, 22(2): 154-165 CrossRef
  14. Feldman N., Rotter-Maskowitz A., Okun E. DAMPs as mediators of sterile inflammation in aging-related pathologies. Ageing Research Reviews, 2015, 24(Pt A): 29-39 CrossRef
  15. Denning N.L., Aziz M., Gurien S.D., Wang P. DAMPs and NETs in sepsis. Front. Immunol., 2019, 10: 2536 CrossRef
  16. Wen S., Li X., Ling Y., Chen S., Deng Q., Yang L., Li Y, Shen J, Qiu Y., Zhan Y., Lai H., Zhang X., Ke Z., Huang W. HMGB1-associated necroptosis and Kupffer cells M1 polarization underlies remote liver injury induced by intestinal ischemia/reperfusion in rats. FASEB J., 2020, 34(3): 4384-4402 CrossRef
  17. Baeuerle P.A., Baltimore D. Activation of DNA-binding activity in an apparently cytoplasmic precursor of the NF-κB transcription factor. Cell, 1988, 53(2): 211-217 CrossRef
  18. Humphries F., Yang S., Wang B., Moynagh P.N. RIP kinases: key decision makers in cell death and innate immunity. Cell Death Differ., 2015, 22(2): 225-236 CrossRef
  19. Kaparakis-Liaskos M. The intracellular location, mechanisms and outcomes of NOD1 signaling. Cytokine, 2015, 74(2): 207-212 CrossRef
  20. Tan Y., Kagan J.C. Innate immune signaling organelles display natural and programmable signaling flexibility. Cell, 2019, 177(2): 384-398.E11 CrossRef
  21. Everts B., Amiel E., Huang S.C., Smith A.M., Chang C.H., Lam W.Y., Redmann V., Freitas T.C., Blagih J., van der Windt G.J., Artyomov M.N., Jones R.G., Pearce E.L., Pearce E.J. TLR-driven early glycolytic reprogramming via the kinases TBK1-IKKɛ supports the anabolic demands of dendritic cell activation. Nat. Immunol., 2014, 15(4): 323-332 CrossRef
  22. Murugina N.E., Budikhina A.S., Dagil Y.A., Maximchik P.V., Balyasova L.S., Murugin V. V., Melnikov M.V., Sharova V.S., Nikolaeva A.M., Chkadua G.Z., Pinegin B.V., Pashenkov M.V. Glycolytic reprogramming of macrophages activated by NOD1 and TLR4 agonists: no association with proinflammatory cytokine production in normoxia. Journal of Biological Chemistry, 2020, 295(10): 3099-3114 CrossRef
  23. Tiedje C., Holtmann H., Gaestel M.. The role of mammalian MAPK signaling in regulation of cytokine mRNA stability and translation. Journal of Interferon & Cytokine Research, 2014, 34(4): 220-232 CrossRef
  24. Günthner R., Kumar V.R.S., Lorenz G., Anders H.J., Lech M. Pattern-recognition receptor signaling regulator mRNA expression in humans and mice, and in transient inflammation or progressive fibrosis. Int. J. Mol. Sci., 2013, 14(9): 18124-18147 CrossRef
  25. Sladek Z., Rysanek D. Expression of macrophage CD44 receptor in the course of experimental inflammatory response of bovine mammary gland induced by lipopolysaccharide and muramyl dipeptide. Research in Veterinary Science, 2009, 86(2): 235-240 CrossRef
  26. Maurić Maljković M., Vlahek I., Piplica A., Ekert Kabalin A., Sušić V., Stevanović V. Prospects of toll-like receptors in dairy cattle breeding. Animal Genetics, 2023, 54(4): 425-434 CrossRef
  27. Moretti I.F., Franco D.G., de Almeida Galatro T.F., Oba-Shinjo S.M., Marie S.K.N. Plasmatic membrane toll-like receptor expressions in human astrocytomas. PLoS One, 2018, 13(6): e0199211 CrossRef
  28. Heil F., Ahmad-Nejad P., Hemmi H., Hochrein H., Ampenberger F., Gellert T., Dietrich H, Lipford G, Takeda K, Akira S, Wagner H, Bauer S. The Toll-like receptor 7 (TLR7)-specific stimulus loxoribine uncovers a strong relationship within the TLR7, 8 and 9 subfamily. Eur. J. Immunol, 2003, 33(11): 2987-2997 CrossRef
  29. Matsumoto M., Funami K., Tanabe M., Oshiumi H., Shingai M., Seto Y., Yamamoto A., Seya T. Subcellular localization of Toll-like receptor 3 in human dendritic cells. J. Immunol., 2003, 171(6): 3154-3162 CrossRef
  30. Kagan J.C., Su T., Horng T., Chow A., Akira S., Medzhitov R. TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-β. Nat. Immunol., 2008, 9(4): 361-368 CrossRef
  31. Lee S.M.Y., Yip T.F., Yan S., Jin D.Y., Wei H.L., Guo R.T., Peiris J.S.M. Recognition of double-stranded RNA and regulation of interferon pathway by toll-like receptor 10. Front. Immunol., 2018, 9: 516 CrossRef
  32. Napetschnig J., Wu H. Molecular basis of NF-κB signaling. Annual Review of Biophysics, 2013, 42(1): 443-468 CrossRef
  33. Gangloff M. Different dimerisation mode for TLR4 upon endosomal acidification? Trends in Biochemical Sciences, 2012, 37(3): 92-98 CrossRef
  34. Goldammer T., Zerbe H., Molenaar A., Schuberth H.J., Brunner R.M., Kata S.R., Seyfert H.M. Mastitis increases mammary mRNA abundance of beta-defensin 5, toll-like-receptor 2 (TLR2), and TLR4 but not TLR9 in cattle. Clinical and Vaccine Immunology, 2004, 11(1): 174-185 CrossRef
  35. Rainard P., Fromageau A., Cunha P., Gilbert F.B. Staphylococcus aureus lipoteichoic acid triggers inflammation in the lactating bovine mammary gland. Vet. Res., 2008, 39(5): 52 CrossRef
  36. Porcherie A., Cunha P., Trotereau A., Roussel P., Gilbert F.B., Rainard P., Germon P. Repertoire of Escherichia coli agonists sensed by innate immunity receptors of the bovine udder and mammary epithelial cells. Vet. Res., 2012, 43(1): 14 CrossRef
  37. Raetz C.R.H., Whitfield C. Lipopolysaccharide endotoxins. Annual Review of Biochemistry, 2002, 71(1): 635-700 CrossRef
  38. Ibeagha-Awemu E.M., Lee J.W., Ibeagha A.E., Bannerman D.D., Paape M.J., Zhao X. Bacterial lipopolysaccharide induces increased expression of toll-like receptor (TLR) 4 and downstream TLR signaling molecules in bovine mammary epithelial cells. Vet. Res., 2008, 39(2): 11 CrossRef
  39. Kauf A.C.W., Vinyard B.T., Bannerman D.D. Effect of intramammary infusion of bacterial lipopolysaccharide on experimentally induced Staphylococcus aureus intramammary infection. Res. Vet. Sci., 2007, 82(1): 39-46 CrossRef
  40. Deng Y., Liu B., Fu C., Gao L., Shen Y., Liu K., Li Q., Cao J., Mao W. Lipopolysaccharide stimulates bovine endometrium explants through toll‑like receptor 4 signaling and PGE2 synthesis. Prostaglandins Leukot Essent Fatty Acids, 2021, 168: 102272 CrossRef
  41. Guo J., Chang G., Zhang K., Xu L., Jin D., Bilal M.S., Shen X. Rumen-derived lipopolysaccharide provoked inflammatory injury in the liver of dairy cows fed a high-concentrate diet. Oncotarget, 2017, 8: 46769-46780 CrossRef
  42. Fuchs K., Cardona Gloria Y., Wolz O., Herster F., Sharma L., Dillen C.A., Täumer C., Dickhöfer S., Bittner Z., Dang T.M., Singh A., Haischer D., Schlöffel M.A., Koymans K.J., Sanmuganantham T., Krach M., Roger T., Le Roy D., Schilling N.A., Frauhammer F., Miller L.S., Nürnberger T., LeibundGut-Landmann S., Gust A.A., Macek B., Frank M., Gouttefangeas C., Dela Cruz C.S., Hartl D., Weber A.N. The fungal ligand chitin directly binds TLR2 and triggers inflammation dependent on oligomer size. EMBO Rep., 2018, 19(12): e46065 CrossRef
  43. Wagener J., Malireddi R.K.S., Lenardon M.D., Köberle M., Vautier S., MacCallum D.M., Biedermann T., Schaller M., Netea M.G., Kanneganti T.D., Brown G.D., Brown A.J., Gow N.A. Fungal chitin dampens inflammation through IL-10 induction mediated by NOD2 and TLR9 activation. PLoS Pathog., 2014, 10(4): e1004050 CrossRef
  44. Chai L.Y.A., Kullberg B.J., Vonk A.G., Warris A., Cambi A., Latgé J.P., Joosten L.A., van der Meer J.W., Netea M.G. Modulation of Toll-like receptor 2 (TLR2) and TLR4 responses by Aspergillus fumigatus. Infection and Immunity, 2009, 77(5): 2184-2192 CrossRef
  45. Monari C., Bistoni F., Casadevall A., Pericolini E., Pietrella D., Kozel T.R., Vecchiarelli A. Glucuronoxylomannan, a microbial compound, regulates expression of costimulatory molecules and production of cytokines in macrophages. The Journal of Infectious Diseases, 2005, 191(1): 127-137 CrossRef
  46. Miyazato A., Nakamura K., Yamamoto N., Mora-Montes H.M., Tanaka M., Abe Y., Tanno D., Inden K., Gang X., Ishii K., Takeda K., Akira S., Saijo S., Iwakura Y., Adachi Y., Ohno N., Mitsutake K., Gow N.A., Kaku M., Kawakami K. Toll-like receptor 9-dependent activation of myeloid dendritic cells by deoxynucleic acids from Candida albicans. Infection and Immunity, 2009, 77(7): 3056-3064 CrossRef
  47. Bond R. Superficial veterinary mycoses. Clinics in Dermatology, 2010, 28(2): 226-236 CrossRef
  48. Farnsworth R.J. Significance of fungal mastitis. J. Am. Vet. Med. Assoc., 1977, 170(10 Pt 2): 1173-1174.
  49. Saini P., Singh M., Kumar P. Fungal endometritis in bovines. Open Veterinary Journal, 2019, 9(1): 94-98 CrossRef
  50. Shandilya U.K., Wu X., McAllister C., Mutharia L., Karrow N.A. Role of Toll-like receptor 4 in Mycobacterium avium subsp. paratuberculosis infection of bovine mammary epithelial (MAC-T) cells in vitro. Microbiology Spectrum, 2023, 11(2): e0439322 CrossRef
  51. Bakshi M., Hebert D., Gulbronson C., Bauchan G., Tuo W., Zarlenga D. Ostertagia ostertagi mediates early host immune responses via macrophage and Toll-like receptor pathways. Infection and Immunity, 2021, 89(6): e00017-21 CrossRef
  52. Zhu J., Brownlie R., Liu Q., Babiuk L.A., Potter A., Mutwiri G.K. Characterization of bovine Toll-like receptor 8: Ligand specificity, signaling essential sites and dimerization. Molecular Immunology, 2009, 46(5): 978-990 CrossRef
  53. Marin M.S., Quintana S., Faverín C., Leunda M.R., Odeón A.C., Pérez S.E. Toll-like receptor activation and expression in bovine alpha-herpesvirus infections. Research in Veterinary Science, 2014, 96(1): 196-203 CrossRef
  54. Ma Y., Wang L., Jiang X., Yao X., Huang X., Zhou K., Yang Y., Wang Y., Sun X., Guan X., Xu Y. Integrative transcriptomics and proteomics analysis provide a deep insight into bovine viral diarrhea virus-host interactions during BVDV infection. Front. Immunol., 2022, 13: 862828 CrossRef
  55. Farias M.V.N., Lendez P.A., Marin M., Quintana S., Martínez-Cuesta L., Ceriani M.C., Dolcini G.L. Toll-like receptors, IFN-γ and IL-12 expression in bovine leukemia virus-infected animals with low or high proviral load. Research in Veterinary Science, 2016, 107: 190-195 CrossRef
  56. Kant R., de Vos W.M., Palva A., Satokari R. Immunostimulatory CpG motifs in the genomes of gut bacteria and their role in human health and disease. J. Med. Microbiol., 2014, 63(2): 293-308 CrossRef
  57. Griebel P.J., Brownlie R., Manuja A., Nichani A., Mookherjee N., Popowych Y., Mutwiri G., Hecker R., Babiuk L.A. Bovine toll-like receptor 9: a comparative analysis of molecular structure, function and expression. Veterinary Immunology and Immunopathology, 2005, 108(1-2): 11-16 CrossRef
  58. Barton G.M., Medzhitov R. Toll-like receptors and their ligands. In: Toll-like receptor family members and their ligands. Current topics in microbiology and immunology, vol. 270. B. Beutler, H. Wagner (eds.). Springer, Berlin, Heidelberg, 2002: 81-92 CrossRef
  59. Li D., Wu M. Pattern recognition receptors in health and diseases. Signal Transduction and Targeted Therapy, 2021, 6(1): 291 CrossRef
  60. Inohara N., Koseki T., del Peso L., Hu Y., Yee C., Chen S., Carrio R., Merino J., Liu D., Ni J., Núñez G. Nod1, an apaf-1-like activator of caspase-9 and nuclear factor-κB. Journal of Biological Chemistry, 1999, 274(21): 14560-14567 CrossRef
  61. Magnuson G., Khan P., Yuan H., Brown B., Divlianska D.B., Stonich D., Peddibhotla M., Su Y., Dad S., Sergienko E., Chung T.D.Y., Roth G.P., Wimer C., Diaz P., Correa R.G., Reed J.C. High throughput screening assays for NOD1 inhibitors — probe 1. In: Probe reports from the NIH molecular libraries program. Bethesda (MD), National Center for Biotechnology Information (US), 2010.
  62. Inohara N., Nuñez G. NODs: intracellular proteins involved in inflammation and apoptosis. Nat. Rev. Immunol., 2003, 3(5): 371-382 CrossRef
  63. Mishra S.K., Dubey P.K., Dhiman A., Dubey S., Verma D., Kaushik A.C., Singh R., Niranjan S.K., Vohra V., Mehrara K.L., Kataria R.S. Sequence-based structural analysis and evaluation of polymorphism in buffalo Nod-like receptor-1 gene. 3 Biotech, 2019, 9(1): 26 CrossRef
  64. Maekawa S., Ohto U., Shibata T., Miyake K., Shimizu T. Crystal structure of NOD2 and its implications in human disease. Nat. Commun., 2016, 7(1): 11813 CrossRef
  65. Inohara N., Koseki T., Lin J., del Peso L., Lucas P.C., Chen F.F., Ogura Y, Núñez G. An induced proximity model for NF-κB activation in the Nod1/RICK and RIP signaling pathways. Journal of Biological Chemistry, 2000, 275(36): 27823-27831 CrossRef
  66. Wu X., Yang Z.H., Wu J., Han J. Ribosome-rescuer PELO catalyzes the oligomeric assembly of NOD-like receptor family proteins via activating their ATPase enzymatic activity. Immunity, 2023, 56(5): 926-943.E7 CrossRef
  67. Bougarn S., Cunha P., Harmache A., Fromageau A., Gilbert F.B., Rainard P. Muramyl dipeptide synergizes with Staphylococcus aureus lipoteichoic acid to recruit neutrophils in the mammary gland and to stimulate mammary epithelial cells. Clinical and Vaccine Immunology, 2010, 17(11): 1797-1809 CrossRef
  68. Bonkobara M., Hoshino M., Yagihara H., Tamura K., Isotani M., Tanaka Y., Washizu T., Ariizumi K. Identification and gene expression of bovine C-type lectin dectin-2. Veterinary Immunology and Immunopathology, 2006, 110(1-2): 179-186 CrossRef
  69. Holder A., Kolakowski J., Rosentreter C., Knuepfer E., Jégouzo S.A.F., Rosenwasser O., Harris H., Baumgaertel L., Gibson A., Werling D. Characterisation of the bovine C-type lectin receptor Mincle and potential evidence for an endogenous ligand. Front. Immunol., 2023, 14: 1189587 CrossRef
  70. Drouin M., Saenz J., Chiffoleau E. C-type lectin-like receptors: head or tail in cell death immunity. Front. Immunol., 2020, 11: 251 CrossRef
  71. Yamasaki S., Ishikawa E., Sakuma M., Hara H., Ogata K., Saito T. Mincle is an ITAM-coupled activating receptor that senses damaged cells. Nat. Immunol., 2008, 9(10): 1179-1188 CrossRef
  72. Brown G.D., Willment J.A., Whitehead L. C-type lectins in immunity and homeostasis. Nat. Rev. Immunol., 2018, 18(6): 374-389 CrossRef
  73. Leteux C., Chai W., Loveless R.W., Yuen C.T., Uhlin-Hansen L., Combarnous Y., Jankovic M., Maric S.C., Misulovin Z., Nussenzweig M.C., Feizi T. The cysteine-rich domain of the macrophage mannose receptor is a multispecific lectin that recognizes chondroitin sulfates A and B and sulfated oligosaccharides of blood group Lewis(a) and Lewis(x) types in addition to the sulfated N-glycans of lutropin. J. Exp. Med., 2000, 191(7): 1117-1126 CrossRef
  74. Stappers M.H.T., Clark A.E., Aimanianda V., Bidula S., Reid D.M., Asamaphan P., Hardison S.E., Dambuza I.M., Valsecchi I., Kerscher B., Plato A., Wallace C.A., Yuecel R., Hebecker B., da Glória Teixeira Sousa M., Cunha C., Liu Y., Feizi T., Brakhage A.A., Kwon-Chung K.J., Gow N.A.R., Zanda M., Piras M., Zanato C., Jaeger M., Netea M.G., van de Veerdonk F.L., Lacerda J.F., Campos A., Carvalho A., Willment J.A., Latgé J.P., Brown G.D. Recognition of DHN-melanin by a C-type lectin receptor is required for immunity to Aspergillus. Nature, 2018, 555(7696): 382-386 CrossRef
  75. Feinberg H., Jégouzo S.A.F., Rex M.J., Drickamer K., Weis W.I., Taylor M.E. Mechanism of pathogen recognition by human dectin-2. Journal of Biological Chemistry, 2017, 292(32): 13402-13414 CrossRef
  76. Wang X., Gong P., Zhang X., Li S., Lu X., Zhao C., Yu Q., Wei Z., Yang Y., Liu Q., Yang Z., Li J., Zhang X. NLRP3 Inflammasome participates in host response to Neospora caninum infection. Front. Immunol., 2018, 9: 1791 CrossRef
  77. Wicherska‐Pawłowska K., Wróbel T., Rybka J. Toll‐like receptors (Tlrs), nod‐like receptors (nlrs) and rig‐i‐like receptors (rlrs) in innate immunity. tlrs, nlrs and rlrs ligands as immunotherapeutic agents for hematopoietic diseases. Int. J. Mol. Sci., 2021, 22(24): 13397 CrossRef
  78. Kawai T., Akira S. Toll-like receptor and RIG-1-like receptor signaling. Ann. N. Y. Acad. Sci, 2008, 1143(1): 1-20 CrossRef
  79. Paul P.S., Lyoo Y.S. Immunogens of rotaviruses. Veterinary Microbiology, 1993, 37(3-4): 299-317 CrossRef
  80. de Verdier Klingenberg K., Svensson L. Group a rotavirus as a cause of neonatal calf enteritis in Sweden. Acta Vet. Scand, 1998, 39(2): 195-199 CrossRef
  81. Novák K., Bjelka M., Samake K., Valčíková T. Potential of TLR-gene diversity in Czech indigenous cattle for resistance breeding as revealed by hybrid sequencing. Arch. Anim. Breed, 2019, 62(2): 477-490 CrossRef
  82. Kalashnikov A.E., Gosteva E.R., Shchegolkov N.F., Yaluga V.L. Vestnik NGAU (Novosibirskiy gosudarstvennyy agrarnyy universitet), 2023, 3: 204-216 CrossRef (in Russ.).
  83. Wang X.P., Luoreng Z.M., Gao S.X., Guo D.S., Li J.Y., Gao X., Xu S.Z., Li F., Chen G., Wang J.R. Haplotype analysis of TLR4 gene and its effects on milk somatic cell score in Chinese commercial cattle. Mol. Biol. Rep., 2014, 41(4): 2345-2351 CrossRef
  84. de Mesquita A.Q., e Rezende C.S.M., de Mesquita A.J., Jardim E.A.G. da V., Kipnis A.P.J. Association of TLR4 polymorphisms with subclinical mastitis in Brazilian holsteins. Braz. J. Microbiol., 2012, 43(2): 692-697 CrossRef
  85. Russell C.D., Widdison S., Leigh J.A., Coffey T.J. Identification of single nucleotide polymorphisms in the bovine Toll-like receptor 1 gene and association with health traits in cattle. Vet. Res., 2012, 43(1): 17 CrossRef
  86. Elmaghraby M.M., El-Nahas A.F., Fathala M.M., Sahwan F.M., Tag EL-Dien M.A. Association of toll-like receptors 2 and 6 polymorphism with clinical mastitis and production traits in Holstein cattle. Iranian Journal of Veterinary Research, Shiraz University, 2018, 19(3): 202-207 CrossRef
  87. Prakash O., Kumar A., Sonwane A., Rathore R., Singh R.V., Chauhan A., Kumar P., Renjith R., Yadav R., Bhaladhare A., Baqir M., Sharma D. Polymorphism of cytokine and innate immunity genes associated with bovine brucellosis in cattle. Mol. Biol. Rep., 2014, 41(5): 2815-2825 CrossRef
  88. Fisher C.A., Bhattarai E.K., Osterstock J.B., Dowd S.E., Seabury P.M., Vikram M., Whitlock R.H., Schukken Y.H., Schnabel R.D., Taylor J.F., Womack J.E., Seabury C.M. Evolution of the bovine TLR gene family and member associations with Mycobacterium avium subspecies paratuberculosis infection. PLoS One, 2011, 6(11): e27744 CrossRef
  89. Mucha R., Bhide M.R., Chakurkar E.B., Novak M., Mikula I. Toll-like receptors TLR1, TLR2 and TLR4 gene mutations and natural resistance to Mycobacterium avium subsp. paratuberculosis infection in cattle. Veterinary Immunology and Immunopathology, 2009, 128(4): 381-388 CrossRef
  90. Cinar M.U., Hizlisoy H., Akyüz B., Arslan K., Aksel E.G., Gümüşsoy K.S. Polymorphisms in toll-like receptor (TLR) 1, 4, 9 and SLC11A1 genes and their association with paratuberculosis susceptibility in Holstein and indigenous crossbred cattle in Turkey. J. Genet., 2018, 97(5): 1147-1154 CrossRef
  91. Bhaladhare A., Sharma D., Kumar A., Sonwane A., Chauhan A., Singh R., Kumar P., Yadav R., Baqir M., Bhushan B., Prakash O. Single nucleotide polymorphisms in toll-like receptor genes and case-control association studies with bovine tuberculosis. Veterinary World, 2016, 9(5): 458-464 CrossRef
  92. Novak K., Kalashnikov A.E., Kalashnikova L.A., Yaluga V.L., Sel’kova I.V., Zakharov V.M. Problemy biologii produktivnykh zhivotnykh, 2021, 2: 22-37 (in Russ.).
  93. Kalashnikov A.E., Gladyr’ E.A., Novikov A.A., Yaluga V.L., Prozherin V.P., Furaeva N.S., Novak K. Zootekhniya, 2019; 9: 2-4 CrossRef (in Russ.).
  94. Bjelka M., Novák K. Association of TLR gene variants in a Czech Red Pied cattle population with reproductive traits. Veterinary Immunology and Immunopathology, 2020, 220: 109997 CrossRef
  95. Vázquez P., Ruiz-Larrañaga O., Garrido J.M., Iriondo M., Manzano C., Agirre M., Estonba A., Juste R.A. Genetic association analysis of paratuberculosis forms in holstein-friesian cattle. Veterinary Medicine International, 2014, 2014: 321327 CrossRef
  96. Seabury C.M., Seabury P.M., Decker J.E., Schnabel R.D., Taylor J.F., Womack J.E. Diversity and evolution of 11 innate immune genes in Bos taurus taurus and Bos taurus indicus cattle. Proceedings of the National Academy of Sciences, 2010, 107(1): 151-156 CrossRef
  97. Dhiman A., Mishra S.K., Dubey P.K., Goyal S., Sehgal M., Niranjan S.K., Sodhi M., Mishra B.P., Kataria R.S. Identification of genetic variation in NOD-like receptor 2 gene and influence of polymorphism on gene structure and function in buffalo (Bubalus bubalis). Research in Veterinary Science, 2017, 115: 43-50 CrossRef
  98. Okuni J.B., Afayoa M., Ojok L. Survey of candidate single-nucleotide polymorphisms in SLC11A1, TLR4, NOD2, PGLYRP1, and IFNγ in Ankole Longhorn cattle in Central region of Uganda to determine their role in Mycobacterium avium subspecies paratuberculosis infection outcome. Front. Vet. Sci., 2021, 8: 614518 CrossRef

 

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