Protection of sheep against experimental footrot by vaccination with pili purified from<i>Bacteroides</i>nodosus

Every, D.; Skerman, T. M.

doi:10.1080/00480169.1982.34921

Cited by 57 publications

(26 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…D. nodosus fimbriae are highly immunogenic, with agglutination reactions involving the fimbrial antigens providing the basis of the classification of D. nodosus into nine major serogroups designated A to I (4). Vaccination of sheep with whole cells of D. nodosus or with purified fimbriae protects against the disease, although this protection is serogroup specific (8,12,13). Multivalent recombinant fimbrial vaccines have been prepared by overexpression of each of the nine fimbrial subunit genes in Pseudomonas aeruginosa (9).…”

mentioning

confidence: 99%

The Type IV Fimbrial Subunit Gene ( fimA ) of Dichelobacter nodosus Is Essential for Virulence, Protease Secretion, and Natural Competence

et al. 2001

View full text Add to dashboard Cite

Dichelobacter nodosus is the essential causative agent of footrot in sheep. The major D. nodosus-encoded virulence factors that have been implicated in the disease are type IV fimbriae and extracellular proteases. To examine the role of the fimbriae in virulence, allelic exchange was used to insertionally inactivate the fimA gene, which encodes the fimbrial subunit protein, from the virulent type G D. nodosus strain VCS1703A. Detailed analysis of two independently derived fimA mutants revealed that they no longer produced the fimbrial subunit protein or intact fimbriae and did not exhibit twitching motility. In addition, these mutants were no longer capable of undergoing natural transformation and did not secrete wild-type levels of extracellular proteases. These effects were not due to polar effects on the downstream fimB gene because insertionally inactivated fimB mutants were not defective in any of these phenotypic tests. Virulence testing of the mutants in a sheep pen trial conducted under controlled environmental conditions showed that the fimA mutants were avirulent, providing evidence that the fimA gene is an essential D. nodosus virulence gene. These studies represent the first time that molecular genetics has been used to determine the role of virulence genes in this slow growing anaerobic bacterium.

show abstract

mentioning

confidence: 99%

The Type IV Fimbrial Subunit Gene ( fimA ) of Dichelobacter nodosus Is Essential for Virulence, Protease Secretion, and Natural Competence

et al. 2001

View full text Add to dashboard Cite

show abstract

“…Infection is spread among sheep grazing on wet pasture (1,8,31). Although antibody titers after infection are insufficient to provide protection against future infections (7, 11), effective immunity against homologous serogroups can be induced by vaccination with either killed whole cells (6, 7) or purified pili-the major host-protective immunogen (13,(38)(39)(40)(41).The pili of B. nodosus are flexible filamentous structures 5 to 6 nm in diameter and up to 10 ,m in length (12,37,46). They have a mainly polar distribution on the cell and, in common with pili from bacterial species as diverse as Pseudomonas aeruginosa, Neisseria gonorrhoeae, Moraxella nonliquefaciens, and Moraxella bovis, are composed of identical subunits of the protein pilin, which has a molecular weight of -18,000 (12,15,18,21,34).…”

mentioning

confidence: 99%

mentioning

confidence: 99%

Nucleotide sequence of the gene encoding the two-subunit pilin of Bacteroides nodosus 265

Elleman¹,

Hoyne²,

McKern³

1986

J Bacteriol

View full text Add to dashboard Cite

The nucleotide sequence of the gene encoding pilin from Bacteroides nodosus 265 has been determined. The pilin is encoded by a single-copy gene, from which can be predicted a prepilin comprising a single protein chain of Mr 16,637. The prepilin sequence differs in several respects from the mature protein sequence. Seven additional N-terminal amino acid residues are present in prepilin, whereas residue 8, phenylalanine, undergoes posttranslational modification to become the N-methylated amino-terminal residue of mature pilin. In addition, further processing occurs through internal cleavage to produce two noncovalently linked subunits characteristic of pilins from serogroup H of B. nodosus, of which strain 265 is a member. The position of cleavage has been identified between alanine residues at positions 72 and 73 of the mature 149-residue pilin protein. The predicted pilin sequence of B. nodosus 265 shows extensive N-terminal amino acid sequence homology with other pilins of the N-methylphenylalanine type. In addition this sequence also shows homology with these N-methylphenylalanine-type pilins in the C-terminal region of the molecule, especially with pilin from Pseudomonas aeruginosa PAK.Bacteroides nodosus is the causative organism of ovine footrot. Infection is spread among sheep grazing on wet pasture (1,8,31). Although antibody titers after infection are insufficient to provide protection against future infections (7, 11), effective immunity against homologous serogroups can be induced by vaccination with either killed whole cells (6, 7) or purified pili-the major host-protective immunogen (13,(38)(39)(40)(41).The pili of B. nodosus are flexible filamentous structures 5 to 6 nm in diameter and up to 10 ,m in length (12,37,46). They have a mainly polar distribution on the cell and, in common with pili from bacterial species as diverse as Pseudomonas aeruginosa, Neisseria gonorrhoeae, Moraxella nonliquefaciens, and Moraxella bovis, are composed of identical subunits of the protein pilin, which has a molecular weight of -18,000 (12,15,18,21,34). Pilin proteins from these bacterial species show extensive homology in their N-terminal amino acid sequences (23), and all begin with the modified amino acid N-methylphenylalanine (NMePhe). Gene sequence studies indicate that the mature protein is produced as a prepilin with six or seven additional Nterminal residues (9, 21, 26, 29). These highly homologous pili are referred to as the NMePhe type; they differ considerably in structure and sequence from the several types of pili found among members of the Enterobacteriaceae (14,30,44,45).At least eight serogroups of B. nodosus (designated A through H) have been identified on the basis of immunological cross-reactivity (3). We have reported previously the gene sequence (9) and the amino acid sequence (23) MATERIALS AND METHODSPreparation of DNA and pili from B. nodosus. B. nodosus 265 was harvested from modified Eugon broth (3) after anaerobic growth for 2 days at 37°C. DNA and pili were prepared as previously described...

show abstract

“…The fimbriae also represent the primary antigenic structures mediating the serological Kagglutination reaction (14,51,57), which has been used to classify field isolates of B. nodosus into at least eight major serogroups and 16 serotypes (6,9,28,46). Correspondingly, the range of effective immunity conferred by vaccination of sheep with either whole cells or isolated fimbriae appears to be restricted to the serogroup involved (10,16,52).…”

mentioning

confidence: 99%

“…This anaerobe contains surface filaments (50,57), termed fimbriae (40), which are now well established as playing a central role in protective immunity against footrot (16,52). The fimbriae also represent the primary antigenic structures mediating the serological Kagglutination reaction (14,51,57), which has been used to classify field isolates of B. nodosus into at least eight major serogroups and 16 serotypes (6,9,28,46).…”

mentioning

confidence: 99%

Variation in the structural subunit and basal protein antigens of Bacteroides nodosus fimbriae

Anderson¹,

Kristo²,

Egerton³

et al. 1986

J Bacteriol

View full text Add to dashboard Cite

The fimbriae of Bacteroides nodosus play a major role in protective immunity against ovine footrot and are an important determinant in the serological classification system that divides field isolates into at least eight serogroups and 16 serotypes. Purified fimbriae contain two polypeptide antigens, the structural subunit of the fimbrial strand (molecular weight about 17,000) and a basal protein (molecular weight about 80,000), both of which exhibit structural variation. Fimbriae were prepared from all prototype strains, as well as from a number of other isolates representative of each of the B. nodosus serotypes, and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Substantial variation was observed in the electrophoretic mobility of the fimbrial subunits from the prototypes of each of the eight serogroups. With the exception of serogroup H, which is an unusual case, the apparent molecular weights of the fimbrial subunits ranged from about 16,500 in serogroup D to 19,000 in serogroup F (serotype 1); in serogroup A, B, C and E, the apparent molecular weights were clustered in the range of 17,000 to 17,500, whereas serogroup G was about 18,500. Serogroup H fimbriae appeared to consist of two smaller polypeptides, which in the prototype (H1) had apparent molecular weights of about 6,000 and 10,000 and which seem to have arisen as a consequence of an internal proteolytic nick in the original subunit. Electrophoretic variation in the fimbrial subunit was also observed between different serotypes, although with the exceptions of serogroups F and H, this was not as pronounced as between the serogroups. Examination of a number of isolates classified within the same serotypes showed that some variation, although minor, also occurred at this level. The basal antigen exhibited significant variation at all levels of the serotypic hierarchy in a manner apparently unrelated to the classification system. Among the range of isolates examined, the apparent molecular weight of this antigen varied from about 77,000 to 88,000.

show abstract

Protection of sheep against experimental footrot by vaccination with pili purified fromBacteroidesnodosus

Cited by 57 publications

References 15 publications

The Type IV Fimbrial Subunit Gene ( fimA ) of Dichelobacter nodosus Is Essential for Virulence, Protease Secretion, and Natural Competence

The Type IV Fimbrial Subunit Gene ( fimA ) of Dichelobacter nodosus Is Essential for Virulence, Protease Secretion, and Natural Competence

Nucleotide sequence of the gene encoding the two-subunit pilin of Bacteroides nodosus 265

Variation in the structural subunit and basal protein antigens of Bacteroides nodosus fimbriae

Contact Info

Product

Resources

About