Plague virulence antigens from Yersinia enterocolitica

Carter, P B; Zahorchak, Robert J.; Brubaker, R R

doi:10.1128/iai.28.2.638-640.1980

Cited by 97 publications

(8 citation statements)

References 9 publications

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“…This energy expenditure is similar to that for other secretion systems such as the type III secretion system (T3SS) [100]. The activity of the T3SS significantly slows down bacterial growth [101–104], and it is reasonable to believe that the same is true for the T6SS. However, although this assumption was included in models [26, 27], it has not yet been experimentally proven.…”

Section: Energetic Costs and Loss Of T6sssmentioning

confidence: 59%

Presence and absence of type VI secretion systems in bacteria

et al. 2022

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The type VI secretion system (T6SS) is a molecular puncturing device that enables Gram-negative bacteria to kill competitors, manipulate host cells and take up nutrients. Who would want to miss such superpowers? Indeed, many studies show how widespread the secretion apparatus is among microbes. However, it is becoming evident that, on multiple taxonomic levels, from phyla to species and strains, some bacteria lack a T6SS. Here, we review who does and does not have a type VI secretion apparatus and speculate on the dynamic process of gaining and losing the secretion system to better understand its spread and distribution across the microbial world.

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Section: Energetic Costs and Loss Of T6sssmentioning

confidence: 59%

Presence and absence of type VI secretion systems in bacteria

et al. 2022

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“…Carter et al (11) have shown that these antigens are also produced by Y. enterocolitica WA at 37°C in a Ca2+-deficient medium containing 20 mM Mg2+; however, it was not reported whether the presence of calcium represses the production of V and W antigens.…”

Section: Resultsmentioning

confidence: 99%

“…To further test whether V antigen is produced under our cultural conditions (TSB, 37°C, 18 h), the cytosol of strain WA was tested against monospecific anti-V serum (obtained from R. R. Brubaker, Michigan State University) and WA-SAA by the gel diffusion technique described by Carter et al (11). The cytosol was obtained from a sonicated cell extract centrifuged at 48,000 x g for 1 h and adjusted to 1.4 mg of protein per ml.…”

Section: Resultsmentioning

confidence: 99%

Serological Relatedness of Mouse-Virulent Yersinia enterocolitica

1982

Infect Immun

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An antiserum (WA-SAA) was produced which agglutinated specifically with mouse-virulent but not with avirulent strains of Yersinia enterocolitica. Expression of the antigenic determinant(s) reacting with WA-SAA was temperature dependent; for growth temperatures of 20 to 40°C, agglutination titers were lowest for cultures grown at 20°C and highest for cultures grown at 35 to 40°C. Addition of Ca2+ (2.5 to 10 mM) to the growth medium had little effect on the agglutination titer, and gel diffusion studies with monospecific anti-V serum indicated that V antigen was not likely to be the determinant reacting with WA-SAA. Immunohistological studies of Peyer's patches of mice infected with Y. entero(olitica WA revealed that the antigenic determinant(s) reacting with WA-SAA was expressed in vivo. The strong correlation of agglutination titer with mouse virulence and the expression in vivo of the antigenic determinant(s) reacting with WA-SAA suggest that the antigen(s) may be associated with the pathogenicity of Y. enterocolitica.Yersinia enterocolitica is a widely distributed organism which may be isolated from a variety of foods. Examples include milk (17, 30), fish (20), porcine tongues (12), chicken (23), lamb (15), beef (15), oysters (1,25), shrimp (25), crab (25), and vegetables used in salads (1). Although the organism is often present in foods and the environment, a large number of the strains isolated from these sources are apparently avirulent (21, 28, 29). Hence, it would be useful to identify characteristics common among virulent Y. enterocolitica that may be used as determinants for developing methods to differentiate virulent from avirulent strains.Several established or presumed virulence determinants have been associated with Yersinia pestis. Included are the ability to produce V and W antigens, capsular or fraction 1 antigen, pesticin, coagulase, and fibrinolysin, and the capacity to absorb hemin (5). Carter et al. ( 11) have shown that mouse-virulent Y. enterocolitica WA produces V and W antigens that are immunologically identical to the V and W antigens of Y. pestis. These are the only virulence determinants known to be common to these two species; however, it is not known whether V and W antigens are common among all strains of mouse-virulent Y. enterocolitica. Interestingly, although not a determinant of virulence, susceptibility to pesticin, a bacteriocin produced by wild-type strains of Yersinia pestis (4), is also a characteristic common among strains of Y. enterocolitica that are lethal to mice (16).We report here a serological test that identi-

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“…Other significant interaction partners of the pilotin outside the T3SS are FtsZ, a prokaryotic tubulin homolog with a key role in cell division, the protease Lon, components of the ATP synthase (subunits α, β, γ), the Sec export pathway (SecF/A), and LolD/E, two components of the ABC transporter of the Lol lipoprotein export pathway in the IM. FtsZ is an interesting interactor, as it might play a role in the long‐known, but still incompletely understood link between T3SS activity and cell growth and division (actively secreting bacteria of many species cease growth and division and are often bigger than T3SS‐deficient or non‐secreting bacteria (Carter et al., 1980; Milne‐Davies et al., 2019; Sasakawa et al., 1986; Sturm et al., 2011)). Notably, although pilotin mutants secrete effectors, they display no secretion‐associated growth inhibition (Figure S4b).…”

Section: Discussionmentioning

confidence: 99%

Pilotins are mobile T3SS components involved in assembly and substrate specificity of the bacterial type III secretion system

Wimmi,

Fleck,

Helbig

et al. 2024

Molecular Microbiology

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In animal pathogens, assembly of the type III secretion system injectisome requires the presence of so‐called pilotins, small lipoproteins that assist the formation of the secretin ring in the outer membrane. Using a combination of functional assays, interaction studies, proteomics, and live‐cell microscopy, we determined the contribution of the pilotin to the assembly, function, and substrate selectivity of the T3SS and identified potential new downstream roles of pilotin proteins. In absence of its pilotin SctG, Yersinia enterocolitica forms few, largely polar injectisome sorting platforms and needles. Accordingly, most export apparatus subcomplexes are mobile in these strains, suggesting the absence of fully assembled injectisomes. Remarkably, while absence of the pilotin all but prevents export of early T3SS substrates, such as the needle subunits, it has little effect on secretion of late T3SS substrates, including the virulence effectors. We found that although pilotins interact with other injectisome components such as the secretin in the outer membrane, they mostly localize in transient mobile clusters in the bacterial membrane. Together, these findings provide a new view on the role of pilotins in the assembly and function of type III secretion injectisomes.

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Plague virulence antigens from Yersinia enterocolitica

Cited by 97 publications

References 9 publications

Presence and absence of type VI secretion systems in bacteria

Presence and absence of type VI secretion systems in bacteria

Serological Relatedness of Mouse-Virulent Yersinia enterocolitica

Pilotins are mobile T3SS components involved in assembly and substrate specificity of the bacterial type III secretion system

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