Bacterial Cell Surface Structures in Yersinia enterocolitica

Białas, Nataniel; Kasperkiewicz, Katarzyna; Radziejewska‐Lebrecht, Joanna; Skurnik, Mikael

doi:10.1007/s00005-012-0168-z

Cited by 33 publications

(29 citation statements)

References 108 publications

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“…The nature of this stabilization is uncertain as no major structural changes have been observed, but it leads to greatly decreased proteolysis of RovA (Uliczka et al, 2011). Nonetheless, despite the large amount of invasin expressed at 25 and 37°C by the O:3 strain, cell invasion is significantly reduced or does not occur at all for bacteria pregrown at 25°C (Bialas et al, 2012). This appears to be because high expression of the O-antigen in the LPS (lipopolysaccharide) creates steric hindrance that prevents interactions between invasin and the host cell surface whereas at 37°C expression of O-antigen is repressed allowing better access of invasin to host cells.…”

Section: Invasin–the First Adhesin Expressed During Invasion Of Entermentioning

confidence: 99%

Yersinia infection tools—characterization of structure and function of adhesins

Mikula¹,

Kolodziejczyk²,

Goldman³

2013

Front. Cell. Inf. Microbio.

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Among the seventeen species of the Gram-negative genus Yersinia, three have been shown to be virulent and pathogenic to humans and animals—Y. enterocolitica, Y. pseudotuberculosis, and Y. pestis. In order to be so, they are armoured with various factors that help them adhere to tissues and organelles, cross the cellular barrier and escape the immune system during host invasion. The group of proteins that mediate pathogen–host interactions constitute adhesins. Invasin, Ail, YadA, YadB, YadC, Pla, and pH 6 antigen belong to the most prominent and best-known Yersinia adhesins. They act at different times and stages of infection complementing each other by their ability to bind a variety of host molecules such as collagen, fibronectin, laminin, β1 integrins, and complement regulators. All the proteins are anchored in the bacterial outer membrane (OM), often forming rod-like or fimbrial-like structures that protrude to the extracellular milieu. Structural studies have shown that the anchor region forms a β-barrel composed of 8, 10, or 12 antiparallel β-strands. Depending on the protein, the extracellular part can be composed of several domains belonging to the immunoglobulin fold superfamily, or form a coiled-coil structure with globular head domain at the end, or just constitute several loops connecting individual β-strands in the β-barrel. Those extracellular regions define the activity of each adhesin. This review focuses on the structure and function of these important molecules, and their role in pathogenesis.

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Section: Invasin–the First Adhesin Expressed During Invasion Of Entermentioning

confidence: 99%

Yersinia infection tools—characterization of structure and function of adhesins

Mikula¹,

Kolodziejczyk²,

Goldman³

2013

Front. Cell. Inf. Microbio.

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“…Also in Africa it is of high importance to develop hygienic practices for poultry food production [22]. Yersinias are typically derived from animals, such as pigs and rodents, and certain strains may cause yersiniosis both in animals and humans [23][24][25]. They were, therefore, not found from field samples in this study.…”

Section: Pmeu In Detecting Pathogens and Antibiotic Resistant Strain mentioning

confidence: 99%

“…[9] and anaerobic salmonellas [6]. Also relatively slow-growing environmental mycobacteria have been rapidly enriched in [11][12][13][14][15][16][17][18][19][20][21][22][23][24] h with the PMEU [10]. This technology has also proven to be highly amenable for field use [11].…”

Section: Introductionmentioning

confidence: 99%

Development of microbiological field methodology for water and food-chain hygiene analysis of Campylobacter spp. and Yersinia spp. in Burkina Faso, West Africa

et al. 2014

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“…Biotype 1A, which is the most heterogeneous one, is generally considered to be nonpathogenic; however, a few studies indicate that some strains might cause gastroenteritis (3)(4)(5)(6). The six biotypes are further divided by serotyping into more than 50 different O groups, defined on the basis of their O-surface antigen in the lipopolysaccharide membrane (7). Human yersiniosis is mainly associated with bioserotypes 1B/O:8, 2/O:5,27, 2/O:9, and 4/O:3.…”

mentioning

confidence: 99%

Rapid Subtyping of Yersinia enterocolitica by Matrix-Assisted Laser Desorption Ionization–Time of Flight Mass Spectrometry (MALDI-TOF MS) for Diagnostics and Surveillance

2013

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In this study, an alternative to the current traditional bioserotyping techniques was developed for subtyping Y. enterocolitica using matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS). The most common pathogenic bioserotypes could easily be distinguished using only a few bioserotype-specific biomarkers. However, biochemical methods should still be used to distinguish biotype 1A from 1B.

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Bacterial Cell Surface Structures in Yersinia enterocolitica

Cited by 33 publications

References 108 publications

Yersinia infection tools—characterization of structure and function of adhesins

Yersinia infection tools—characterization of structure and function of adhesins

Development of microbiological field methodology for water and food-chain hygiene analysis of Campylobacter spp. and Yersinia spp. in Burkina Faso, West Africa

Rapid Subtyping of Yersinia enterocolitica by Matrix-Assisted Laser Desorption Ionization–Time of Flight Mass Spectrometry (MALDI-TOF MS) for Diagnostics and Surveillance

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