scholarly journals Role of YadA, Ail, and Lipopolysaccharide in Serum Resistance of Yersinia enterocolitica Serotype O:3

2005 ◽  
Vol 73 (4) ◽  
pp. 2232-2244 ◽  
Author(s):  
Marta Biedzka-Sarek ◽  
Reija Venho ◽  
Mikael Skurnik
Keyword(s):  
Yersinia Enterocolitica ◽  
Alternative Pathway ◽  
Outer Membrane Proteins ◽  
Outer Core ◽  
Normal Serum ◽  
Serum Resistance ◽  
Bacterial Killing ◽  
Term Survival ◽  
O Antigen ◽  
Serotype O

ABSTRACT Complement attack is a host strategy leading to elimination of pathogens. Yersinia enterocolitica expresses several potential complement resistance factors: the outer membrane proteins YadA and Ail as well as lipopolysaccharide (LPS). To study the contribution of these factors to the survival of Y. enterocolitica serotype O:3 in nonimmune human serum, we constructed 23 mutant strains of Y. enterocolitica O:3 expressing different combinations of YadA, Ail, LPS O antigen, and LPS outer core. Survival of bacteria was analyzed in normal serum (with functional classical, lectin, and alternative complement activation pathways) and EGTA-Mg-treated serum (only alternative pathway functional). Kinetic killing tests revealed that the most potent single-serum resistance factor needed for long-term survival was YadA; Ail was also indispensable, but it provided short-term survival and delayed the bacterial killing. On the contrary, the LPS O antigen and outer core, when in combination with YadA, Ail, or both, had a minor and often negative effect on serum resistance. Bacteria in the exponential phase of growth were more resistant to serum killing than stationary-phase bacteria. After exposing bacteria to EGTA-Mg-treated serum, O antigen could prevent deposition of covalently bound C3b on bacteria at 3 min of incubation, even as a single factor. At later time points (15 and 30 min) it had to be accompanied by YadA, Ail, and outer core. In normal serum, the bacteria were less resistant to C3b deposition. However, no direct correlation between the C3 deposition pattern and bacterial resistance was observed.

scholarly journals Functional Mapping of YadA- and Ail-Mediated Binding of Human Factor H to Yersinia enterocolitica Serotype O:3

2008 ◽  
Vol 76 (11) ◽  
pp. 5016-5027 ◽  
Author(s):  
Marta Biedzka-Sarek ◽  
Saara Salmenlinna ◽  
Markus Gruber ◽  
Andrei N. Lupas ◽  
Seppo Meri ◽  
...  
Keyword(s):  
Yersinia Enterocolitica ◽  
Alternative Pathway ◽  
Outer Membrane Proteins ◽  
Factor H ◽  
Complement Alternative Pathway ◽  
Human Host ◽  
Serotype O ◽  
Complement Resistance ◽  
Sense And Respond ◽  
Active Complement

ABSTRACT Yersinia enterocolitica is an enteric pathogen that exploits diverse means to survive in the human host. Upon Y. enterocolitica entry into the human host, bacteria sense and respond to variety of signals, one of which is the temperature. Temperature in particular has a profound impact on Y. enterocolitica gene expression, as most of its virulence factors are expressed exclusively at 37°C. These include two outer membrane proteins, YadA and Ail, that function as adhesins and complement resistance (CR) factors. Both YadA and Ail bind the functionally active complement alternative pathway regulator factor H (FH). In this study, we characterized regions on both proteins involved in CR and the interaction with FH. Twenty-eight mutants having short (7 to 41 amino acids) internal deletions within the neck and stalk of YadA and two complement-sensitive site-directed Ail mutants were constructed to map the CR and FH binding regions of YadA and Ail. Functional analysis of the YadA mutants revealed that the stalk of YadA is required for both CR and FH binding and that FH appears to target several conformational and discontinuous sites of the YadA stalk. On the other hand, the complement-sensitive Ail mutants were not affected in FH binding. Our results also suggested that Ail- and YadA-mediated CR does not depend solely on FH binding.

scholarly journals The mechanisms of complement activation in normal bovine serum and normal horse serum against Yersinia enterocolitica O:9 strains with different outer membrane proteins content

2016 ◽  
Vol 19 (1) ◽  
pp. 99-107 ◽  
Author(s):  
K. Miętka ◽  
K. Brzostek ◽  
K. Guz-Regner ◽  
G. Bugla-Płoskońska
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Yersinia Enterocolitica ◽  
Bactericidal Activity ◽  
Complement Activation ◽  
Alternative Pathway ◽  
Outer Membrane Proteins ◽  
Serum Resistance ◽  
Main Role ◽  
Wild Type

AbstractYersinia enterocolitica is a common zoonotic pathogen and facultative intracellular bacterium which can survive within blood cells. Cattle and horses are considered a reservoir of Y. enterocolitica which often causes several serious syndromes associated with yersiniosis such as abortions, premature births or infertility. The aim of our investigation was to determine the vitality of Y. enterocolitica O:9 strains (Ye9) in bovine and horse sera (NBS and NHrS) and explain the role of outer membrane proteins (OMPs) in serum resistance of these bacteria. Our previous studies demonstrated moderate human serum (NHS) resistance of the wild type Ye9 strain, whereas mutants lacking YadA, Ail or OmpC remained sensitive to the bactericidal activity of NHS. The present study showed that the wild type of Ye9 strain was resistant to the bactericidal activity of both NHrS and NBS, while Ye9 mutants lacking the YadA, Ail and OmpC proteins were sensitive to NHrS and NBS as well as to NHS. The mechanisms of complement activation against Ye9 strains lacking Ail and YadA were distinguished, i.e. activation of the classical/lectin pathways decisive in the bactericidal mechanism of complement activation of NBS, parallel activation of the classical/lectin and alternative pathways of NHrS. In this research the mechanism of independent activation of the classical/lectin or the alternative pathway of NBS and NHrS against Ye9 lacking OmpC porin was also established. The results indicate that serum resistance of Ye9 is multifactorial, in which extracellular structures, i.e. outer membrane proteins (OMPs) such as Ail, OmpC or YadA, play the main role.

scholarly journals Yersiniophage ϕR1-37 is a tailed bacteriophage having a 270 kb DNA genome with thymidine replaced by deoxyuridine

Microbiology ◽  
2005 ◽  
Vol 151 (12) ◽  
pp. 4093-4102 ◽  
Author(s):  
Saija Kiljunen ◽  
Kristo Hakala ◽  
Elise Pinta ◽  
Suvi Huttunen ◽  
Patrycja Pluta ◽  
...  
Keyword(s):  
Yersinia Pseudotuberculosis ◽  
Burst Size ◽  
Outer Core ◽  
International Committee ◽  
Amino Acid Sequences ◽  
Structural Proteins ◽  
Virulence Plasmid ◽  
O Antigen ◽  
Serotype O ◽  
Phage Receptor

Bacteriophage ϕR1-37 was isolated based on its ability to infect strain YeO3-R1, a virulence-plasmid-cured O antigen-negative derivative of Yersinia enterocolitica serotype O : 3. In this study, the phage receptor was found to be a structure in the outer core hexasaccharide of Y. enterocolitica O : 3 LPS. The phage receptor was present in the outer core of strains of many other Y. enterocolitica serotypes, but also in some Yersinia intermedia strains. Surprisingly, the receptor structure resided in the O antigen of Yersinia pseudotuberculosis O : 9. Electron microscopy demonstrated that ϕR1-37 particles have an icosahedral head of 88 nm, a short neck of 10 nm, a long contractile tail of 236 nm, and tail fibres of at least 86 nm. This implies that the phage belongs to the order Caudovirales and the family Myoviridae in the ICTV (International Committee for Taxonomy of Viruses) classification. ϕR1-37 was found to have a lytic life cycle, with eclipse and latent periods of 40 and 50 min, respectively, and a burst size of ∼80 p.f.u. per infected cell. Restriction digestions and PFGE showed that the ϕR1-37 genome was dsDNA and ∼270 kb in size. Enzymically hydrolysed DNA was subjected to HPLC-MS/MS analysis, which demonstrated that the ϕR1-37 genome is composed of DNA in which thymidine (T) is >99 % replaced by deoxyuridine (dU). The only organisms known to have similar DNA are the Bacillus subtilis-specific bacteriophages PBS1 and PBS2. N-terminal amino acid sequences of four major structural proteins did not show any similarity to (viral) protein sequences in databases, indicating that close relatives of ϕR1-37 have not yet been characterized. Genes for two of the structural proteins, p24 and p46, were identified from the partially sequenced ϕR1-37 genome.

scholarly journals Differentiation between serological responses to Brucella suis and Yersinia enterocolitica serotype O[ratio ]9 after natural or experimental infection in pigs

2005 ◽  
Vol 134 (2) ◽  
pp. 347-357 ◽  
Author(s):  
G. JUNGERSEN ◽  
V. SØRENSEN ◽  
S. B. GIESE ◽  
J. A. STACK ◽  
U. RIBER
Keyword(s):  
Yersinia Enterocolitica ◽  
Experimental Infection ◽  
False Positive ◽  
Indirect Elisa ◽  
Serum Samples ◽  
Cross Sectional ◽  
O Antigen ◽  
Serotype O ◽  
Brucella Suis ◽  
Limited Period

False-positive serological reactions (FPSR) due to infections with Yersinia enterocolitica serotype O[ratio ]9 (YeO[ratio ]9) are a problem in tests for brucellosis. In the present study, FPSR in classical and novel tests for brucellosis following experimental infections of pigs with YeO[ratio ]9 were compared with responses of B. suis biovar 2-inoculated pigs. FPSR were limited to 2–9 weeks post-YeO[ratio ]9 inoculation, while B. suis-infected pigs were test-positive throughout the 21-week period of investigation. Although YeO[ratio ]9-inoculated pigs exhibited FPSR in Brucella tests for a limited period of time, the serological responses in a YeO[ratio ]9-purified O-antigen indirect ELISA did not decrease accordingly. Analysis of available cross-sectional serum samples from pig herds naturally infected with YeO[ratio ]9 or B. suis biovar 2 confirmed that the observed difference in the duration of the serological responses between the two infections could be used to discriminate between herds infected with B. suis biovar 2 and YeO[ratio ]9.

scholarly journals Molecular and chemical characterization of the lipopolysaccharide O‐antigen and its role in the virulence of Yersinia enterocolitica serotype O:8

1997 ◽  
Vol 23 (1) ◽  
pp. 63-76 ◽  
Author(s):  
Lijuan Zhang ◽  
Joanna Radziejewska‐Lebrecht ◽  
Danuta Krajewska‐Pietrasik ◽  
Paavo Toivanen ◽  
Mikael Skurnik
Keyword(s):  
Yersinia Enterocolitica ◽  
Chemical Characterization ◽  
O Antigen ◽  
Serotype O

scholarly journals Characterization of Complement Factor H Binding to Yersinia enterocolitica Serotype O:3

2008 ◽  
Vol 76 (9) ◽  
pp. 4100-4109 ◽  
Author(s):  
Marta Biedzka-Sarek ◽  
Hanna Jarva ◽  
Heidi Hyytiäinen ◽  
Seppo Meri ◽  
Mikael Skurnik
Keyword(s):  
Yersinia Enterocolitica ◽  
Outer Core ◽  
Factor H ◽  
Negative Regulator ◽  
Complement Factor ◽  
Short Consensus Repeats ◽  
Serotype O ◽  
Complement Resistance ◽  
Number Of Bacteria

ABSTRACT A number of bacteria bind factor H (FH), the negative regulator of the alternative complement pathway, to avoid complement-mediated killing. Here we show that a gram-negative enteric pathogen, Yersinia enterocolitica serotype O:3, uses two virulence-related outer membrane (OM) proteins to bind FH. With Y. enterocolitica O:3 mutant strains displaying different combinations of surface factors relevant to complement resistance, we demonstrated that the major receptor for FH is the OM protein YadA. Another OM protein, Ail, also contributes to FH binding provided that it is not blocked by distal parts of the lipopolysaccharide (i.e., the O antigen and the outer core hexasaccharide). Importantly, we demonstrated that surface-bound FH was functional; both YadA- and Ail-bound FH displayed cofactor activity for factor I-mediated cleavage of C3b. With truncated recombinant FH constructs, we located the binding site of Ail specifically to short consensus repeats 6 and 7 of FH, while YadA showed a novel type of FH-binding pattern and appears to bind FH throughout the entire FH molecule. We thus conclude that Y. enterocolitica, via YadA and Ail, recruits functionally active FH to its surface. FH binding appears to be an important mechanism of the complement resistance of this pathogen.

scholarly journals The lipopolysaccharide outer core of Yersinia enterocolitica serotype O:3 is required for virulence and plays a role in outer membrane integrity

1999 ◽  
Vol 31 (5) ◽  
pp. 1443-1462 ◽  
Author(s):  
Mikael Skurnik ◽  
Reija Venho ◽  
Jose-Antonio Bengoechea ◽  
Ignacio Moriyon
Keyword(s):  
Outer Membrane ◽  
Yersinia Enterocolitica ◽  
Membrane Integrity ◽  
Outer Core ◽  
Serotype O
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