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. 1992 Jul;60(7):2992–2994. doi: 10.1128/iai.60.7.2992-2994.1992

Interaction of ruminant transferrins with transferrin receptors in bovine isolates of Pasteurella haemolytica and Haemophilus somnus.

R H Yu 1, S D Gray-Owen 1, J Ogunnariwo 1, A B Schryvers 1
PMCID: PMC257264  PMID: 1612764

Abstract

The interactions of ruminant transferrins with receptors on bovine isolates of Pasteurella haemolytica and Haemophilus somnus were compared by growth studies and direct and competitive binding assays. Isolates of P. haemolytica were capable of utilizing and binding transferrin from sheep, goat, or cattle, whereas isolates of H. somnus were capable of utilizing and binding only bovine transferrin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baldwin G. S., Weinstock J. Nucleotide sequence of porcine liver transferrin. Nucleic Acids Res. 1988 Sep 12;16(17):8720–8720. doi: 10.1093/nar/16.17.8720. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bártek J., Viklický V., Franek F., Angelisová P., Dráber P., Jarosíková T., Nemec M., Verlová H. Monoclonal antibodies against transferrin. Precipitating mixtures and lack of inter-species cross-reactivity. Immunol Lett. 1982 May;4(5):231–235. doi: 10.1016/0165-2478(82)90043-8. [DOI] [PubMed] [Google Scholar]
  3. Bártek J., Viklický V., Stratil A. Phylogenetically more conservative epitopes among monoclonal antibody-defined antigenic sites of human transferrin are involved in receptor binding. Br J Haematol. 1985 Mar;59(3):435–441. doi: 10.1111/j.1365-2141.1985.tb07330.x. [DOI] [PubMed] [Google Scholar]
  4. Dyer D. W., West E. P., McKenna W., Thompson S. A., Sparling P. F. A pleiotropic iron-uptake mutant of Neisseria meningitidis lacks a 70-kilodalton iron-regulated protein. Infect Immun. 1988 Apr;56(4):977–983. doi: 10.1128/iai.56.4.977-983.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gonzalez G. C., Caamano D. L., Schryvers A. B. Identification and characterization of a porcine-specific transferrin receptor in Actinobacillus pleuropneumoniae. Mol Microbiol. 1990 Jul;4(7):1173–1179. doi: 10.1111/j.1365-2958.1990.tb00692.x. [DOI] [PubMed] [Google Scholar]
  6. Metz-Boutigue M. H., Jollès J., Mazurier J., Schoentgen F., Legrand D., Spik G., Montreuil J., Jollès P. Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins. Eur J Biochem. 1984 Dec 17;145(3):659–676. doi: 10.1111/j.1432-1033.1984.tb08607.x. [DOI] [PubMed] [Google Scholar]
  7. Ogunnariwo J. A., Cheng C., Ford J., Schryvers A. B. Response of Haemophilus somnus to iron limitation: expression and identification of a bovine-specific transferrin receptor. Microb Pathog. 1990 Dec;9(6):397–406. doi: 10.1016/0882-4010(90)90058-x. [DOI] [PubMed] [Google Scholar]
  8. Ogunnariwo J. A., Schryvers A. B. Iron acquisition in Pasteurella haemolytica: expression and identification of a bovine-specific transferrin receptor. Infect Immun. 1990 Jul;58(7):2091–2097. doi: 10.1128/iai.58.7.2091-2097.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Schryvers A. B. Characterization of the human transferrin and lactoferrin receptors in Haemophilus influenzae. Mol Microbiol. 1988 Jul;2(4):467–472. doi: 10.1111/j.1365-2958.1988.tb00052.x. [DOI] [PubMed] [Google Scholar]
  11. Schryvers A. B., Gonzalez G. C. Comparison of the abilities of different protein sources of iron to enhance Neisseria meningitidis infection in mice. Infect Immun. 1989 Aug;57(8):2425–2429. doi: 10.1128/iai.57.8.2425-2429.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Schryvers A. B., Lee B. C. Comparative analysis of the transferrin and lactoferrin binding proteins in the family Neisseriaceae. Can J Microbiol. 1989 Mar;35(3):409–415. doi: 10.1139/m89-063. [DOI] [PubMed] [Google Scholar]
  13. Schryvers A. B., Morris L. J. Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis. Infect Immun. 1988 May;56(5):1144–1149. doi: 10.1128/iai.56.5.1144-1149.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Schryvers A. B., Morris L. J. Identification and characterization of the transferrin receptor from Neisseria meningitidis. Mol Microbiol. 1988 Mar;2(2):281–288. doi: 10.1111/j.1365-2958.1988.tb00029.x. [DOI] [PubMed] [Google Scholar]
  15. Tsai J., Dyer D. W., Sparling P. F. Loss of transferrin receptor activity in Neisseria meningitidis correlates with inability to use transferrin as an iron source. Infect Immun. 1988 Dec;56(12):3132–3138. doi: 10.1128/iai.56.12.3132-3138.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Weinberg E. D. Iron and infection. Microbiol Rev. 1978 Mar;42(1):45–66. doi: 10.1128/mr.42.1.45-66.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]

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