Isotypic antibody responses in cattle infected with Haemophilus somnus

Widders, P. R.; Dowling, Susan; Gogolewski, R P; Smith, James W.; Corbeil, Lynette B.

doi:10.1016/s0034-5288(18)31147-0

Cited by 10 publications

(2 citation statements)

References 15 publications

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“…However, the antiserum tested contained predominantly IgGl antibodies (18). Others have shown that IgG2 is important in protection against pyogenic infections in cattle (36,(50)(51)(52), and our previous experiments with H. somnus infection indicate that IgG2 antibodies are likely to be important in protection against bovine infection with H. somnus also (17,18,54,55). This may be because bovine IgG2 is more opsonic than bovine IgGl (34).…”

Section: Discussionmentioning

confidence: 81%

Characterization of a 78-kilodalton outer membrane protein of Haemophilus somnus

1990

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A 78-kilodalton (kDa) outer membrane protein (OMP) of Haemophilus somnus was one of the two antigens most consistently and most intensely immunoreactive in Western immunoblots of whole cells of H. somnus reacted with convalescent-phase serum obtained from cattle with experimental H. somnus pneumonia. This antigen was isolated by gel filtration chromatography of sodium dodecyl sulfate-solubilized OMP. Reactions of Western blots with bovine monospecific antiserum prepared against the 78-kDa antigen indicated that this 78-kDa OMP was present in each of 22 isolates of H. somnus obtained from cattle with pneumonia, thromboembolic meningoencephalitis, and abortion as well as from vaginal or preputial carriers. The 78-kDa OMP was also present in each isolate obtained weekly throughout the course of experimental H. somnus pneumonia in a calf. Monospecific antiserum to the 78-kDa OMP also reacted with proteins from closely related bacterial species in the family Pasteurellaceae but not with bacteria of 13 other genera. The 78-kDa OMP of H. somnus is of interest because it is surface accessible, highly conserved, immunogenic, cross-reactive with other members of the family Pasteurellaceae, and reactive with convalescent-phase serum which is passively protective against H. somnus pneumonia.

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Section: Discussionmentioning

confidence: 81%

Characterization of a 78-kilodalton outer membrane protein of Haemophilus somnus

1990

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“…Further study indicated passive protection against experimentally induced pneumonia with H. somnus by antibody against the 40-kDa antigen (16). Failure of antiserum against the 78-kDa antigen to provide protection was considered to be due to the lack of immunoglobulin G2 (16), which was suggested to be important in protection against H. somnus infection (55,56).…”

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confidence: 99%

Cloning and sequencing of the gene encoding a 31-kilodalton antigen of Haemophilus somnus

Won

Griffith

1993

Infect Immun

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Immunoblots using bovine antibody against Haemophilus somnus as the primary antibody consistently identified 31-, 40- and 78-kDa proteins in Sarkosyl-insoluble extracts of H. somnus. A genomic library of H. somnus 8025 DNA was constructed in plasmid pUC19, and 45 recombinants expressed proteins which were recognized by bovine antiserum in Western blots (immunoblots). Ten of the recombinants expressing a 31-kDa protein caused the lysis of bovine erythrocytes. Restriction endonuclease mapping indicated that the hemolytic recombinants shared an approximately 1.7-kb BglII fragment. Southern blot analysis using the BglII fragment as a probe revealed homology among the recombinants and the presence of an identically sized BglII fragment in the chromosome of all H. somnus isolates tested. Sequence analysis indicated the presence of an 822-bp open reading frame within the 1.7-kb BglII fragment. Deletion of this open reading frame resulted in the loss of hemolytic activity and protein expression in recombinant Escherichia coli, suggesting the possible role of the 31-kDa protein as a hemolysin. An amino acid sequence deduced from the DNA sequence shared homology with outer membrane protein A of E. coli, Salmonella typhimurium, and Shigella dysenteriae, with P6 of Haemophilus influenzae, and with PIII of Neisseria gonorrhoeae. An amino acid analysis of the recombinant 31-kDa protein agreed with the amino acid composition deduced from the DNA sequence.

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