Degradation of bovine complement C3 by trichomonad extracellular proteinase

S. A. Kania, S. L. Reed, J. W. Thomford, Robert Bondurant, K. Hirata, R. R. Corbeil, M. J. North, L. B. Corbeil

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Bovine trichomoniasis is a local infection of the reproductive tract making interaction with mucosal host defenses crucial. Since the parasite is susceptible to killing by bovine complement, we investigated the role of the third component of complement (C3) in host parasite interactions. Bovine C3 was purified by anionic and cationic exchange chromatography. The purified protein was characterized by immunoreactivity, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and peptide sequencing of the amino terminus of the β chain. When purified bovine C3 was incubated for varying time periods with trichomonad extracellular proteinases, SDS-PAGE gels revealed digestion of the α chain to small fragments. Such degradation in vivo would prevent formation of C3b and completion of the complement cascade, resulting in evasion of killing. To evaluate the relevance of this data, we determined whether C3 was present in bovine genital secretions. With a quantitative ELISA assay, C3 could be demonstrated in both uterine and vaginal washes. To our knowledge, this is the first demonstration of bovine C3 in genital secretions. The C3 concentration increased significantly in vaginal secretions by 8 and 10 weeks in heifers infected with Tritrichomonas foetus. An increase was also seen in uterine secretions of infected heifers, but sample numbers were insufficient for statistical analysis. Transcription of the major extracellular cysteine proteinase (TFCP8) was demonstrated in T. foetus cells from uterine secretions of infected heifers by RT-PCR and Southern blotting. The results indicate that C3 may be important in genital defense and that trichomonad extracellular proteinases may play a role in evasion of complement-mediated killing.

Original languageEnglish (US)
Pages (from-to)83-96
Number of pages14
JournalVeterinary Immunology and Immunopathology
Volume78
Issue number1
DOIs
StatePublished - Jan 10 2001

Fingerprint

Trichomonadida
Complement C3
complement
Peptide Hydrolases
proteinases
secretion
degradation
cattle
Tritrichomonas foetus
genitalia
heifers
Sodium Dodecyl Sulfate
polyacrylamide gel electrophoresis
Polyacrylamide Gel Electrophoresis
Complement C3b
Reproductive Tract Infections
trichomoniasis
Host-Parasite Interactions
Cysteine Proteases
cysteine proteinases

Keywords

  • Complement component 3
  • Extracellular cysteine proteinase
  • Genital secretions
  • Tritrichomonas foetus

ASJC Scopus subject areas

  • Animal Science and Zoology
  • Immunology
  • veterinary(all)

Cite this

Degradation of bovine complement C3 by trichomonad extracellular proteinase. / Kania, S. A.; Reed, S. L.; Thomford, J. W.; Bondurant, Robert; Hirata, K.; Corbeil, R. R.; North, M. J.; Corbeil, L. B.

In: Veterinary Immunology and Immunopathology, Vol. 78, No. 1, 10.01.2001, p. 83-96.

Research output: Contribution to journalArticle

Kania, SA, Reed, SL, Thomford, JW, Bondurant, R, Hirata, K, Corbeil, RR, North, MJ & Corbeil, LB 2001, 'Degradation of bovine complement C3 by trichomonad extracellular proteinase', Veterinary Immunology and Immunopathology, vol. 78, no. 1, pp. 83-96. https://doi.org/10.1016/S0165-2427(00)00256-7
Kania, S. A. ; Reed, S. L. ; Thomford, J. W. ; Bondurant, Robert ; Hirata, K. ; Corbeil, R. R. ; North, M. J. ; Corbeil, L. B. / Degradation of bovine complement C3 by trichomonad extracellular proteinase. In: Veterinary Immunology and Immunopathology. 2001 ; Vol. 78, No. 1. pp. 83-96.
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