Conversion of Type Antigen IV in Shigella Flexneri by Bacteriophage

Iseki, Shoei; Hamano, Sosaku

doi:10.2183/pjab1945.35.407

Cited by 25 publications

(10 citation statements)

References 9 publications

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“…O‐antigen modification in Gram‐negative bacteria by serotype‐converting bacteriophage such as of P22 and bacteriophage of S. flexneri was first described many years ago (Iseki and Kashiwagi, 1955; 1959; for review see Allison and Verma, 2000). The best‐studied systems are the serotype‐converting bacteriophage of S. flexneri , SFII, SF6, SFV and SFX, that carry genes encoding proteins required to glucosylate the O‐antigen of Shigella at unique positions resulting in serotype conversion from serotype Y to serotypes 2a, 3b, 5a and X respectively (Huan et al ., 1997a,b; Guan et al ., 1999; Allison and Verma, 2000).…”

Section: Discussionmentioning

confidence: 99%

‘Form variation’ of the O12 antigen is critical for persistence of Salmonella Typhimurium in the murine intestine

Bogomolnaya¹,

Santiviago²,

Yang³

et al. 2008

Molecular Microbiology

108

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SummarySalmonella enterica subspecies I serotypes are responsible for the vast majority of salmonellosis in mammals and birds, yet only a few factors specific to this group that allow them to persist in this niche have been identified. We show that STM0557, a S. enterica subspecies I-specific gene encoding an inner membrane protein, is critical for faecal shedding and intestinal persistence of S. enterica serotype Typhimurium ATCC14028 in Salmonella-resistant mice, but mutations in this gene do not diminish short-term intestinal colonization or invasion of cultured epithelial cells. STM0557 and two neighbouring genes, located on a pathogenicity island termed SPI-16, resemble genes of the gtrA,B, gtr(type) cluster in seroconverting bacteriophages. In general, the gtr genes encode proteins responsible for serotype conversion of the infected bacterium by addition glucose residues to repeating O-antigen subunits of lipopolysaccharide (LPS). In lysogenized Shigella, such modifications have been previously shown to be constitutively expressed and to facilitate invasion of host cells. We show that serotype Typhimurium gtr orthologues, STM0557-0559, are responsible for 'form variation' or glucosylation of the O12 antigen galactose (4 position) to generate the 12-2 variant. Form variation in Typhimurium is not constitutive, but occurred upon exposure and during intracellular growth of serotype Typhimurium in J774 macrophages. Our data suggest that the 12-2 antigen is a S. enterica subspecies I-specific LPS modification that enhances long-term intestinal colonization, and is in contrast to the role of O-antigen variation described for Shigella.

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Section: Discussionmentioning

confidence: 99%

‘Form variation’ of the O12 antigen is critical for persistence of Salmonella Typhimurium in the murine intestine

Bogomolnaya¹,

Santiviago²,

Yang³

et al. 2008

Molecular Microbiology

108

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“…Type IV phage, which modifies GlcNAc with an ␣-linked glucosyl residue, was first identified by Matsui (1958), who found that the lysate of a 4c strain could change the serotype of a type I strain to a type IV. This was continued by Iseki and Hamano (1959), who converted a type II strain to a type IV. Only the type IV epitope was present, indicating that one phage had replaced the other.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of bacteriophage SfII‐mediated serotype conversion in Shigella flexneri

Mavris

Manning

Morona

1997

Molecular Microbiology

102

119

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SummaryWe have isolated the lysogenic bacteriophage SfII, which mediates glucosylation of Shigella flexneri Oantigen, resulting in expression of the type II antigen. SfII belongs to group A of the Bradley classification and has a genome size of 42.3 kb. DNA sequencing of a 4 kb BamHI subclone identified four open reading frames (ORFs), of which only two were found to be necessary for serotype conversion. These genes were named bgt, which encodes a putative bactoprenol glucosyl transferase, and gtrII, encoding the putative type II antigen determining glucosyl transferase. These genes are adjacent to the integrase gene (int ) and attachment site (attP ), which are highly homologous to those of Salmonella bacteriophage P22. Another ORF encoded a highly hydrophobic protein of 120 amino acids with homologues in Escherichia coli, Salmonella bacteriophage P22 and S. flexneri. Previous studies identified gtrX, the glucosyl transferase gene, of bacteriophage SfX, which also glucosylates the Oantigen specifically. We determined that gtrX-mediated expression of the group 7,8 antigen also requires bgt. This allowed us to identify gtrII as being the serotype antigen II determining glucosyl transferase. Southern hybridization and polymerase chain reaction (PCR) analyses indicated that bgt homologues exist in the genomes of all S. flexneri serotypes and in E. coli K-12, whereas gtrII was only detected in strains of serotype 2. Transposon TnphoA-derived chromosomal mutations of bgt and gtrII in S. flexneri serotype 2a were isolated and characterized. [ 35 S]-methionine labelling and the use of a T7 RNA polymerase expression system identified a protein of 34 kDa corresponding to Bgt. However, GtrII, which has a predicted molecular weight of 55 kDa, was not detected. We propose that the function of Bgt is to transfer the glucose residues from the UDP-glucose onto bactoprenol and GtrII then transfers the glucose onto the O-antigen repeat unit at the rhamnose III position. The chromosomal organization of these serotype-converting genes, when compared with their homologues in E. coli K-12 chromosome and the P22 bacteriophage genome, were very similar. This suggests that the regions encode similar functions in these organisms and have a similar evolutionary origin.

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“…Matsui (1 958) converted antigens I and I11 of serotypes l a and 3a, respectively, to antigen IV with a phage from serotype 4c. Using the appropriate phages, other workers converted the analogous antigens of la, lb, 2a, 3b and variant Y to IV (Iseki and Hamano, 1959) and those of 2a, 2b, 4a, variant X and variant Y to I (Okada et al, 1960). A variant Y strain was doubly converted to variant X and then serotype 2b by Giammanco (1968) with the two appropriate phages f-7,8 and f-I1 sequentially.…”

Section: Genetic Aspects Of Sjeexneri 0-antigensmentioning

confidence: 99%

Structure and biology of Shigella flexneri O antigens

Simmons

Romanowska

1987

Journal of Medical Microbiology

108

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The species Shigellajiexneri comprises a serologically heterogeneous group of dysentery bacilli whose 0 antigens are polysaccharide-lipid Apolypeptide-lipid B complexes strictly comparable in their gross structural and biological properties to the analogous antigens present in all gram-negative bacilli of the family Enterobacteriaceae (Simmons, 1971a). As shown in fig. 1, the lipopolysaccharide (LPS) component of these antigens comprises two distinct regions-a common basal structure shared by all S . JIexneri serotypes (except serotype 6) and 0-specific side-chains that determine the serological specificity and cross-reactivity of the whole antigen (Simmons, 1966). The common basal sugars 2-keto-3-deoxy-octonate, L-glycero-D-manno-heptose phosphate, D-glucose, D-galactose and Nacetyl-D-glucosamine are incorporated into the growing basal structure in that order and defects in the genes controlling this biosynthetic pathway result in an incomplete basal structure of rough (R) specificity (Johnston et al., 1967). The 0-specific side-chains (each consisting of six to eight repeating pentasaccharide units) may be further subdivided into two regions-a primary unbranched chain of L-rhamnose and N-acetyl-D-glucosamine identical to the variant Y antigen, and secondary side-chains of a-D-glucosyl and 0-acetyl residues which are substituted on the primary chain in a position that is unique for each serotype (Simmons, 1969). The specificity of the linkage of the glucose secondary side-chain is governed by specific UDP-glucose transferases that are phage-dependent and map near the lac locus (Manson et al., 1970). Loss of the phage attachment site in recombination experiments with Escherichia coli HfrC (lac+) strains usually leads to loss of the glucose secondary sidechains and, thus, to the production of lactosefermenting hybrids of variant Y-type specificity (Manson et al., 1970). However, hybrids with other specificities have also been described (Romanowska and Lachowicz, 1970 ;Katzenellenbogen et al., 1973;Lugowski et al., 1975).In an earlier review (Simmons, 197 la), structural and genetic aspects of the biosynthesis of the S. JIexneri 0 antigens were considered in detail. The conclusions drawn at that time about the structural changes involved in smooth to rough (S-+R) mutation, in the production of X and Y variants, and in the modification of type-specificity by lysogenic conversion remain valid today. However, some of the structures themselves require to be revised, largely as a result of methylation studies performed during the past decade by Lindberg and his colleagues (Lindberg et al., 1973;Kenne et al., 1977a and b ;Kenne et al., 1978). This review summarises the evidence for these currently accepted structures and indicates how these studies have elucidated the biology of the S. J-lexneri 0 antigens. Structure of the basal region of S.J-lexneri lipopolysaccharidesThe biosynthesis of the S. jiexneri LPS basal region proceeds from the 2-keto-3-deoxy-octonatelipid A core of chemotype Re by the sequential addition of...

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Conversion of Type Antigen IV in Shigella Flexneri by Bacteriophage

Cited by 25 publications

References 9 publications

‘Form variation’ of the O12 antigen is critical for persistence of Salmonella Typhimurium in the murine intestine

‘Form variation’ of the O12 antigen is critical for persistence of Salmonella Typhimurium in the murine intestine

Mechanism of bacteriophage SfII‐mediated serotype conversion in Shigella flexneri

Structure and biology of Shigella flexneri O antigens

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