Generation of <i>Campylobacter fetus</i> S‐layer protein diversity utilizes a single promoter on an invertible DNA segment

Dworkin, Joel; Blaser, Martin J.

doi:10.1111/j.1365-2958.1996.tb02469.x

Cited by 43 publications

(71 citation statements)

References 51 publications

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“…Cloning and sequencing of the S-protein genes of C. fetus 23D revealed that the different S-proteins originated from multiple S-protein genes. An active S-promoter was found upstream of the S-protein gene (sapA) for the wild-type strain (Dworkin and Blaser, 1996). Inversion of a 6.2 kb chromosomal segment containing the S-promoter leads to the expression of either one of the two S-protein genes (sapA or sapA2 ) surrounding this invertable segment (Fig.…”

Section: S-layer Variation and Silent S-protein Genesmentioning

confidence: 99%

Expression, secretion and antigenic variation of bacterial S‐layer proteins

Boot

Pouwels

1996

Molecular Microbiology

119

108

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SummaryThe function of the S-layer, a regularly arranged structure on the outside of numerous bacteria, appears to be different for bacteria living in different environments. Almost no similarity exists between the primary sequences of S-proteins, although their amino acid composition is comparable. S-protein production is directed by single or multiple promoters in front of the S-protein gene, yielding stable mRNAs. Most bacteria secrete S-proteins via the general secretory pathway (GSP). Translocation of S-protein across the outer membrane of Gram-negative bacteria sometimes occurs by S-protein-specific branches of the GSP. O-polysaccharide side-chains of the lipopolysaccharide component of the cell wall of Gramnegative bacteria appear to function as receptors for attachment of the S-layer. Silent S-protein genes have been found in Campylo-bacter fetus and Lactobacillus acidophilus. These silent genes are placed in the expression site in a fraction of the bacterial population via inversion of a chromosomal segment.

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Section: S-layer Variation and Silent S-protein Genesmentioning

confidence: 99%

Expression, secretion and antigenic variation of bacterial S‐layer proteins

Boot

Pouwels

1996

Molecular Microbiology

119

108

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“…There is also increasing evidence that S-layer-carrying bacteria may use Slayer variation, by expressing alternative S-layer protein genes, for adaptation to different stress factors, such as the immune response of the host for pathogens and drastic changes in the environmental conditions for nonpathogens. In most of the characterized cases, the mechanism of S-layer variation is based on DNA rearrangements (4,8,26,29). Structural features of S layers also indicate that they may offer several advantages for different biotechnological applications.…”

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confidence: 99%

Isolation of Three New Surface Layer Protein Genes ( slp ) from Lactobacillus brevis ATCC 14869 and Characterization of the Change in Their Expression under Aerated and Anaerobic Conditions

Jakava-Viljanen

Åvall-Jääskeläinen

Messner³

et al. 2002

J Bacteriol

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Two new surface layer (S-layer) proteins (SlpB and SlpD) were characterized, and three slp genes (slpB, slpC, and slpD) were isolated, sequenced, and studied for their expression in Lactobacillus brevis neotype strain ATCC 14869. Under different growth conditions, L. brevis strain 14869 was found to form two colony types, smooth (S) and rough (R), and to express the S-layer proteins differently. Under aerobic conditions R-colony type cells produced SlpB and SlpD proteins, whereas under anaerobic conditions S-colony type cells synthesized essentially only SlpB. Anaerobic and aerated cultivations of ATCC 14869 cells in rich medium also resulted in S-layer protein patterns similar to those of the S-and R-colony type cells, respectively. Electron microscopy suggested the presence of only a single S-layer with an oblique structure on the cells of both colony forms. The slpB and slpC genes were located adjacent to each other, whereas the slpD gene was not closely linked to the slpB-slpC gene region. Northern analyses confirmed that both slpB and slpD formed a monocistronic transcription unit and were effectively expressed, but slpD expression was induced under aerated conditions. slpC was a silent gene under the growth conditions tested. The amino acid contents of all the L. brevis ATCC 14869 S-layer proteins were typical of S-layer proteins, whereas their sequence similarities with other S-layer proteins were negligible. The interspecies identity of the L. brevis S-layer proteins was mainly restricted to the Nterminal regions of those proteins. Furthermore, Northern analyses, expression of a PepI reporter protein under the control of the slpD promoter, and quantitative real-time PCR analysis of slpD expression under aerated and anaerobic conditions suggested that, in L. brevis ATCC 14869, the variation of S-layer protein content involves activation of transcription by a soluble factor rather than DNA rearrangements that are typical for most of the S-layer phase variation mechanisms known.Surface layers (S layers) are monomolecular crystalline arrays of proteinaceous subunits present in almost all archaea and all major phylogenetic groups of bacteria (26,33). Most of the S layers are composed of subunits of a single protein or glycoprotein species capable of forming symmetrical arrays and covering the cell surface during all stages of growth. Slayer proteins commonly contain high numbers of acidic and hydrophobic amino acids but lack overall amino acid sequence homology with corresponding proteins from unrelated species. Moreover, a low pI is typical for S-layer proteins (31) except for those from different lactobacilli (5, 40) and Methanothermus fervidus (6). Diverse functions have been proposed for S layers, such as acting as molecular sieves, protective coats, molecular and ion traps, cell shape determinants, and promoters for cell adhesion and surface recognition (26). There is also increasing evidence that S-layer-carrying bacteria may use Slayer variation, by expressing alternative S-layer protein genes, for ada...

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“…Third, mutagenesis studies (Blaser et al, 1994) indicated that SLP expression variation is associated with exchange of cassettes 3Ј to the sapA promoter. Fourth, spontaneous S ¹ mutant strains that have a 9 kb deletion including this promoter (Tummuru and Blaser, 1992;Fujita and Amako, 1994;Dworkin et al, 1995b), are unable to produce an S-layer under any circumstance tested, including strong in vivo and in vitro selection for the S þ phenotype (Dworkin and Blaser, 1996).…”

Section: Nature Of the Sapa Promotermentioning

confidence: 99%

“…Mapping of the phenotypic variants indicated chromosomal rearrangement due to inversion of a long (6.2 kb) segment of DNA containing this promoter (Dworkin and Blaser, 1996). Cloning and sequencing of the 6.2 kb promoter-containing invertible DNA element revealed a probable 5.6 kb operon of four overlapping ORFs of which three have predicted strong amino acid homologies to members of the RTX family of protein secretion (type I) pathway (Thompson et al, 1997).…”

Section: Nature Of the Sapa Promotermentioning

confidence: 99%

“…Incubation in serum selected for survivors expressing an undisrupted SLP gene, which occurred at an approximate frequency of 10 ¹4 . These studies indicated that in addition to the promoter inversion between two oppositely oriented SLP gene cassettes, C. fetus is capable of exchanging one of the SLP cassettes bracketing the invertible element with non-flanking, previously silent, cassettes (Dworkin and Blaser, 1996; (Fig. 2).…”

Section: A Flexible Dna Inversion Mechanismmentioning

confidence: 99%

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Molecular mechanisms of Campylobacter fetus surface layer protein expression

Dworkin

Blaser

1997

Molecular Microbiology

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SummaryCells of the Gram-negative bacteria Campylobacter fetus are covered by monomolecular arrays of surface layer proteins (SLPs) critical for both persistence in their natural hosts and for virulence. For C. fetus cells, expression of SLPs essentially eliminates C3b binding and their antigenic variation thwarts host immunological defences. Each cell possesses multiple partially homologous and highly conserved SLP gene cassettes, tightly clustered in the genome, that encode SLPs of 97-149 kDa. These attach non-covalently via a conserved N-terminus to the cell wall lipopolysaccharide. Recent studies indicate that C. fetus reassorts a single promoter, controlling SLP expression, and one, or more, complete open reading frame strictly by DNA inversion, and that rearrangement is independent of the distance between sites of inversion. In contrast to previously reported programmed DNA inversion systems, inversion in C. fetus is recA-dependent. These rearrangements permit variation in protein expression from the family of SLP genes and suggest an expanding paradigm of programmed DNA rearrangements among microorganisms.

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Generation of Campylobacter fetus S‐layer protein diversity utilizes a single promoter on an invertible DNA segment

Cited by 43 publications

References 51 publications

Expression, secretion and antigenic variation of bacterial S‐layer proteins

Expression, secretion and antigenic variation of bacterial S‐layer proteins

Isolation of Three New Surface Layer Protein Genes ( slp ) from Lactobacillus brevis ATCC 14869 and Characterization of the Change in Their Expression under Aerated and Anaerobic Conditions

Molecular mechanisms of Campylobacter fetus surface layer protein expression

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