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Identified virulence factors of Campylobacter: Adherence


CadF (Campylobacter adhesion to fibronectin)  

Related genes: cadF;
Keywords: Adherence; Invasion; FnBP;
Figures:
Model for C. jejuni-induced signaling leading to Cdc42 activation and bacterial invasion (From: Krause-Gruszczynska M, et al., 2011. The signaling pathway of Campylobacter jejuni-induced Cdc42 activation: Role of fibronectin, integrin beta1, tyrosine kinases and guanine exchange factor Vav2. Cell Commun Signal 9:32.).


Functions:
37 kDa outer-membrane protein mediating the binding of the organism to the extracellular matrix component fibronectin, which in turn stimulates a signal transduction pathway.
References:
Konkel ME, et al., 1997. Identification and molecular cloning of a gene encoding a fibronectin-binding protein (CadF) from Campylobacter jejuni. Mol. Microbiol. 24(5):953-963.
Monteville MR, Konkel ME, 2002. Fibronectin-facilitated invasion of T84 eukaryotic cells by Campylobacter jejuni occurs preferentially at the basolateral cell surface. Infect. Immun. 70(12):6665-6671.
Monteville MR, et al., 2003. Maximal adherence and invasion of INT 407 cells by Campylobacter jejuni requires the CadF outer-membrane protein and microfilament reorganization. Microbiology 149:153-165.
Konkel ME, et al., 2005. Identification of a fibronectin-binding domain within the Campylobacter jejuni CadF protein. Mol. Microbiol. 57(4):1022-1035.
Scott NE, et al., 2010. Mass spectrometric characterization of the Campylobacter jejuni adherence factor CadF reveals post-translational processing that removes immunogenicity while retaining fibronectin binding. Proteomics. 10(2):277-288.


Capsule  

Related genes: Cj1423c; Cj1416c; Cj1421c; Cj1422c; Cj1426c; Cj1427c; Cj1429c; Cj1432c; Cj1433c; Cj1434c; Cj1435c; Cj1436c; Cj1437c; Cj1438c; Cj1440c; Cj1442c; cysC; fcl; glf; gmhA2; hddA; hddC; kfiD; kpsC; kpsD; kpsE; kpsF; kpsM; kpsS; kpsT; rfbC;
Keywords: Adherence; Phase variation;
Characteristics:
Major antigenic component of the classic Penner serotyping system.
Variation in the capsule structure may cause by multiple mechanisms, such as exchange of capsular genes and entire clusters by horizontal transfer, gene duplication, deletion, fusion and the presence of homopolymeric G tracts in several cps genes.
Structure features:
The capsule consists of repeating oligosaccharide units attached to a dipalmitoyl-glycerophosphate lipid anchor.
The CPS is extensively substituted with variable O-methylphosphoramidate, methyl, ethanolamine, and N-glycerol groups.
Functions:
Play an important role in bacterial survival and persistence in the environment and evasion of host immune response.
The presence of heptose residues in the capsule may be important for virulence. Heptose residues found in some cell surface-located glycoconjugates are required for adhesion.
References:
Karlyshev AV, et al., 2000. Genetic and biochemical evidence of a Campylobacter jejuni capsular polysaccharide that accounts for Penner serotype specificity. Mol.Microbiol. 35(3):529-541.
Karlyshev AV, et al., 2001. Detection and initial characterization of novel capsular polysaccharide among diverse Campylobacter jejuni strains using alcian blue dye. J. Clin. Microbiol. 39(1):279-284.
Bacon DJ, et al., 2001. A phase-variable capsule is involved in virulence of Campylobacter jejuni 81-176. Mol. Microbiol. 40(3):769-777.
Karlyshev AV, et al., 2001. Demonstration of polysaccharide capsule in Campylobacter jejuni using electron microscopy. Infect. Immun. 69(9):5921-5924.
St Michael F, et al., 2002. The structures of the lipooligosaccharide and capsule polysaccharide of Campylobacter jejuni genome sequenced strain NCTC 11168. Eur. J. Biochem. 269(21):5119-5136.
Karlyshev AV, et al., 2005. Analysis of Campylobacter jejuni capsular loci reveals multiple mechanisms for the generation of structural diversity and the ability to form complex heptoses. Mol.Microbiol. 55(1):90-103.
Karlyshev AV, et al., 2005. The Campylobacter jejuni glycome. FEMS Microbiol. Rev. 29(2):377-390.


FlpA (Fibronectin-like protein A)  

Keywords: Adherence; FnBP;
Structure features:
FN-binding domain has been localized to nine amino acids [156aa–164aa, Trp-Arg-Pro-His-Pro-Asp-Phe-Arg-Val (WRPHPDFRV)].
Figures:
A model of C. jejuni interaction with host cells (From: Talukdar PK, et al., 2020. Molecular Dissection of the Campylobacter jejuni CadF and FlpA Virulence Proteins in Binding to Host Cell Fibronectin. Microorganisms 8:pii: E389.).


Functions:
Binds to the gelatin-binding domain of FN and activates Erk1/2 signaling.
References:
Konkel ME, et al., 2010. Campylobacter jejuni FlpA binds fibronectin and is required for maximal host cell adherence. J Bacteriol 192:68-76.
Larson CL, et al., 2013. The fibronectin-binding motif within FlpA facilitates Campylobacter jejuni adherence to host cell and activation of host cell signaling. Emerg Microbes Infect 2:e65.


JlpA (jejuni lipoprotein A)  

Related genes: jlpA;
Keywords: Adherence;
Figures:
Hypothetical model for C. jejuni-induced signaling events leading to bacterial invasion and establishing infections (From: O Croinin T, et al., 2012. Host epithelial cell invasion by Campylobacter jejuni: trigger or zipper mechanism? Front Cell Infect Microbiol 2:25.).


Functions:
A surface-exposed and species-specific lipoprotein mediating adherence of the bacterium to epithelial cells.
Mechanism:
May interact with cell surface-exposed Hsp90α to initiate signalling pathways that lead to activation of NF-κB and p38 MAP kinase, two central components in host proinflammatory responses.
References:
Jin S, et al., 2003. JlpA of Campylobacter jejuni interacts with surface-exposed heat shock protein 90alpha and triggers signalling pathways leading to the activation of NF-kappaB and p38 MAP kinase in epithelial cells. Cell Microbiol. 5(3):165-174.
Scott NE, et al., 2009. Mass spectrometric characterization of the surface-associated 42 kDa lipoprotein JlpA as a glycosylated antigen in strains of Campylobacter jejuni. J. Proteome Res. 8(10):4654-4664.


LOS (lipooligosaccharide)  

Related genes: Cj1135; Cj1136; Cj1137c; Cj1138; Cj1144c; Cj1145c; cstIII; gmhA; hldD; hldE; htrB; neuA1; neuB1; neuC1; waaC; waaF; waaV; wlaN;
Keywords: Adherence; Phase variation; Structural mimicry; Immune evasion;
Functions:
LOS diversity is important for the ability to colonize a wide variety of hosts and intestinal niches.
The ability to generate variation at high frequency, the molecular mimicry evident in LOS structure support a role in the avoidance of host defences.
The similarity of LOS structures to host gangliosides and the subsequent ability to generate crossreacting antibodies forms the pathological basis for the association of preceding C. jejuni infection with Guillain-Barre syndrome.
References:
Linton D, et al., 2000. Multiple N-acetyl neuraminic acid synthetase (neuB) genes in Campylobacter jejuni: identification and characterization of the gene involved in sialylation of lipo-oligosaccharide. Mol. Microbiol. 35(5):1120-1134.
Guerry P, et al., 2000. Sialylation of lipooligosaccharide cores affects immunogenicity and serum resistance of Campylobacter jejuni. Infect. Immun. 68(12):6656-6662.
Guerry P, et al., 2002. Phase variation of Campylobacter jejuni 81-176 lipooligosaccharide affects ganglioside mimicry and invasiveness in vitro. Infect. Immun. 70(2):787-793.
Godschalk PC, et al., 2004. The crucial role of Campylobacter jejuni genes in anti-ganglioside antibody induction in Guillain-Barre syndrome. J. Clin. Invest. 114(11):1659-1665.
Heikema AP, et al., 2010. Characterization of the specific interaction between sialoadhesin and sialylated Campylobacter jejuni lipooligosaccharides. Infect. Immun. 78(7):3237-3246.


MOMP (major outer membrane protein)  

Related genes: porA;
Keywords: Adherence;
Functions:
A putative porin and a multifuction surface protein, may play an important role in adherence.
References:
Moser I, et al., 1997. Campylobacter jejuni major outer membrane protein and a 59-kDa protein are involved in binding to fibronectin and INT 407 cell membranes. FEMS Microbiol. Lett. 157(2):233-238.
Zhang Q, et al., 2000. Sequence polymorphism, predicted secondary structures, and surface-exposed conformational epitopes of Campylobacter major outer membrane protein. Infect. Immun. 68(10):5679-5689.


PEB1  

Related genes: pebA;
Keywords: Adherence;
Characteristics:
An aspartate/glutamate-binding protein of an ABC transporter, essential for microaerobic growth on dicarboxylic amino acids.
Functions:
Cell-binding factor, enhancing bacterial adherence to and invasion of host cells.
References:
Pei Z, Blaser MJ, 1993. PEB1, the major cell-binding factor of Campylobacter jejuni, is a homolog of the binding component in gram-negative nutrient transport systems. J. Biol. Chem. 268(25):18717-18725.
Pei Z, et al., 1998. Mutation in the peb1A locus of Campylobacter jejuni reduces interactions with epithelial cells and intestinal colonization of mice. Infect. Immun. 66(3):938-943.
Leon-Kempis Mdel R, et al., 2006. The Campylobacter jejuni PEB1a adhesin is an aspartate/glutamate-binding protein of an ABC transporter essential for microaerobic growth on dicarboxylic amino acids. Mol. Microbiol. 60(5):1262-1275.








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