Nucleotide sequence of the structural gene, tcpA, for a major pilin subunit of Vibrio choleras

Faast, Renate; Ogierman, Monica A.; Stroeher, Uwe H.; Manning, Paul A.

doi:10.1016/0378-1119(89)90486-1

Cited by 75 publications

(46 citation statements)

References 21 publications

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“…Strain, serogroup and source of isolation are listed. GenBank accession numbers : strain Z17561, M33514 (Faast et al, 1989) ; strain HB84419, AY052830 ; strain XJ90006, AY056619 ; strain GX95065, AY056618 ; strain SD95001, AY052831 ; strain SCE188, AF208385 (Mukhopadhyay et al, 2001) ; strain 10259, AF139626 (Nandi et al, 2000) ; strain VCE22, AF414371 ; strain C6709, U09807 (Rhine & Taylor, 1994) ; strain H1, X74730 (Ogierman et al, 1996). Nelson et al (1997) greater than that at the mdh locus or several other V. cholerae chromosomal loci (Table 2).…”

Section: Analysis Of the Genetic Relationships Among Tcpa Allelesmentioning

confidence: 99%

Evolutionary and functional analyses of variants of the toxin-coregulated pilus protein TcpA from toxigenic Vibrio cholerae non-O1/non-O139 serogroup isolates The GenBank accession numbers for the sequences reported in this paper are AY078355–AY078358.

Boyd

Waldor

2002

Microbiology

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The toxin-coregulated pilus (TCP) is a critical determinant of the pathogenicity of Vibrio cholerae. This bundle-forming pilus is an essential intestinal colonization factor and also serves as a receptor for CTXφ, the filamentous phage that encodes cholera toxin (CT). TCP is a polymer of repeating subunits of the major pilin protein TcpA and tcpA is found within the Vibrio pathogenicity island (VPI). In this study genetic variation at the tcpA locus in toxigenic isolates of V. cholerae was investigated and three novel TcpA sequences from V. cholerae strains V46, V52 and V54, belonging to serogroups O141, O37 and O8, respectively, were identified. These novel tcpA alleles grouped into three distinct clonal lineages. The polymorphisms in TcpA were predominantly located in the carboxyl region of TcpA in surface-exposed regions of TCP fibres. Comparison of the genetic diversity among V. cholerae isolates at the tcpA locus with that of aldA, another locus within the VPI, and mdh, a chromosomal locus, revealed that tcpA sequences are far more diverse than these other loci. Most likely, this diversity is a reflection of diversifying selection in adaptation to the host immune response or to CTXφ susceptibility. An assessment of the functional properties of the variant tcpA sequences in the non-O1 V. cholerae strains was carried out by analysing whether these strains could be infected by CTXφ and colonize the suckling mouse. Similar to El Tor strains of V. cholerae O1, in vitro CTXφ infection of these strains required the exogenous expression of toxT, suggesting that in these strains ToxT regulates TCP expression and that these TcpA variants can serve as CTXφ receptors. All the V. cholerae non-O1 serogroup isolates tested were capable of colonizing the suckling mouse small intestine, suggesting that the different TcpA variants could function as colonization factors.

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Section: Analysis Of the Genetic Relationships Among Tcpa Allelesmentioning

confidence: 99%

Evolutionary and functional analyses of variants of the toxin-coregulated pilus protein TcpA from toxigenic Vibrio cholerae non-O1/non-O139 serogroup isolates The GenBank accession numbers for the sequences reported in this paper are AY078355–AY078358.

Boyd

Waldor

2002

Microbiology

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“…The classical type 4 fimbrial subunits from P. aeruginosa, N. gonorrhoeae, M. bovis, D. nodosus and other epithelial pathogens are all sim ilar in size (about 145-160 amino acids) and have a similar overall structure (see Dalrymple and Mattick, 1987). However the toxin co-regulated pili of v. cholerae (Faast et al , 1989;Shaw and Taylor, 1990), the bundle-forming pili of enteropathogenic E. coli (Giron et al, 1991) and the thin pili of E. coli Incl plasmids (Kim and Komano , 1992) seem to represent distinct fimbrial subtypes. Each of these is composed of subunits that show the characteristic type 4 amino terminal sequence (Fig.…”

Section: Morphogenesis Of Surface-associated Protein Complexesmentioning

confidence: 99%

Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein‐secretion apparatus: a general system for the formation of surface‐associated protein complexes

Hobbs

Mattick

1993

Molecular Microbiology

361

286

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Summary The Pseudomonas aeruginosa genes pilB‐D and pilQ are necessary for the assembly of type 4 fimbriae. Homologues of these genes and of the subunit (pilin) gene have been described in various different bacterial species, but not always in association with type 4 fimbrial biosynthesis and function. Pil‐like proteins are also involved in protein secretion, DNA transfer by conjugation and transformation, and morphogenesis of filamentous bacteriophages. It seems likely that the Pil homologues function in the processing and export of proteins resembling type 4 fimbrial sub‐units, and in their organization into fimbrial‐like structures. These may either be true type 4 fimbriae, or components of protein complexes which act in the transport of macromolecules (DNA or protein) into or out of the cell. Some PilB‐like and PilQ‐like proteins are apparently also involved in the assembly of non‐type 4 polymeric structures (filamentous phage virions and conjugative pili). The diverse studies summarized in this review are providing insight into an extensive infrastructural system which appears to be utilized in the formation of a variety of cell surface‐associated complexes.

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“…One piece of evidence that implies a proteolytic cleavage of TcpA emerges from the DNA sequence (Faast et al 1989;Shaw and Taylor 1990). The predicted size of the TcpA leader peptide correlates directly to the 2.5-kD difference between the two forms of TcpA visualized in Western blots.…”

Section: Pulse-chase Analysismentioning

confidence: 99%

Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria.

Kaufman¹,

Seyer²,

Taylor³

1991

Genes Dev.

103

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Biogenesis of the Vibrio cholerae toxin-coregulated pilus (TCP) requires the activities of at least seven accessory proteins. We demonstrate that a portion of this pathway involves a novel processing step in which a hydrophilic leader peptide is proteolytically removed from TcpA by the gene product characterized in this report, TcpJ, to yield the mature, export-competent form of the pilin. Cleavage of the pilin leader peptide is independent of known signal peptidases as demonstrated by pilin-processing profiles in Escherichia coli strains conditionally defective for production of leader peptidase or grown in the presence of the antibiotic globomycin. Additionally, pilin cleavage did not rely on the SecA protein, as evidenced by TcpA processing in azide-treated cells. These results suggest that TcpJ is representative of a new class of proteins involved in SecA-independent proteolytic cleavage of a set of atypical leader peptides during extracellular export.

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Nucleotide sequence of the structural gene, tcpA, for a major pilin subunit of Vibrio choleras

Cited by 75 publications

References 21 publications

Evolutionary and functional analyses of variants of the toxin-coregulated pilus protein TcpA from toxigenic Vibrio cholerae non-O1/non-O139 serogroup isolates The GenBank accession numbers for the sequences reported in this paper are AY078355–AY078358.

Evolutionary and functional analyses of variants of the toxin-coregulated pilus protein TcpA from toxigenic Vibrio cholerae non-O1/non-O139 serogroup isolates The GenBank accession numbers for the sequences reported in this paper are AY078355–AY078358.

Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein‐secretion apparatus: a general system for the formation of surface‐associated protein complexes

Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria.

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