Recognition of B cells epitopes of the Klebsiella pneumoniae GroEL-like protein by HLA-B27 positive subjects

Cancino-Díaz, Mario E.; Ayala-Narváez, Humberto; Burgos‐Vargas, Rubén; Reyes-Lopez, A; Tovar-Castillo, Laura; L, Domínguez-López; Arreola, Julio Granados; Jiménez-Zamudio, L; Garcı́a-Latorre, Ethel

doi:10.1006/mpat.1999.0339

Cited by 10 publications

(4 citation statements)

References 27 publications

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“…GroEL, a cytoplasmic chaperone also known to be a surface associated protein, was the most abundant protein identified in both the outer membrane and OMV of the wbbO strain, and had been identified as a significant component of vesicles from A. baumannii and F. novicida (Kwon et al, 2009;Pierson et al, 2010). While GroEL has classically been considered a cytoplasmic chaperone, there is emerging data demonstrating that this protein can be associated with the outer surface of both Gram-positive and Gram-negative bacterial species (Cancino-Diaz et al, 2000;He and De Buck, 2010;Zhu et al, 2013). Cytoplasmic GroEL functions as a chaperone that modulates protein folding; but surface associated GroEL has been shown to promote host inflammation and phagocytosis of several bacterial species (Garduno et al, 1998;Odenbreit et al, 2006;Zhu et al, 2013).…”

Section: Discussionmentioning

confidence: 98%

“…We focused on the membrane and vesicles from K. pneumoniae, a nosocomial pathogen associated with urinary tract infections, bacteremia, pneumonia, and pyogenic liver abscess (Podschun and Ullmann, 1998;Cancino-Diaz et al, 2000;Evrard et al, 2010;Hsieh et al, 2012). Hospital acquired K. pneumoniae infections have a 50% mortality rate if left untreated, largely due to the rapid acquisition of antibiotic resistance (Nordmann et al, 2009;Evrard et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

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Klebsiella pneumoniae O antigen loss alters the outer membrane protein composition and the selective packaging of proteins into secreted outer membrane vesicles

Cahill

Seeley

Gutel

et al. 2015

Microbiological Research

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Klebsiella pneumoniae is a nosocomial pathogen which naturally secretes lipopolysaccharide (LPS) and cell envelope associated proteins into the environment through the production of outer membrane vesicles (OMVs). The loss of the LPS O antigen has been demonstrated in other bacterial species to significantly alter the composition of OMVs. Therefore, this study aimed to comprehensively analyze the impact of O antigen loss on the sub-proteomes of both the outer membrane and secreted OMVs from K. pneumoniae. As determined by LC-MS/MS, OMVs were highly enriched with outer membrane proteins involved in cell wall, membrane, and envelope biogenesis as compared to the source cellular outer membrane. Deletion of wbbO, the enzyme responsible for O antigen attachment to LPS, decreased but did not eliminate this enrichment effect. Additionally, loss of O antigen resulted in OMVs with increased numbers of proteins involved in post-translational modification, protein turnover, and chaperones as compared to secreted vesicles from the wild type. This alteration of OMV composition may be a compensatory mechanism to deal with envelope stress. This comprehensive analysis confirms the highly distinct protein composition of OMVs as compared to their source membrane, and provides evidence for a selective sorting mechanism that involves LPS polysaccharides. These data support the hypothesis that modifications to LPS alters both the mechanics of protein sorting and the contents of secreted OMVs and significantly impacts the protein composition of the outer membrane.

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Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Klebsiella pneumoniae O antigen loss alters the outer membrane protein composition and the selective packaging of proteins into secreted outer membrane vesicles

Cahill

Seeley

Gutel

et al. 2015

Microbiological Research

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“…Many studies revealed that antibodies against Hsp specifically bind to target tissue of the autoaggressive response. Accumulating evidence from epidemiological or immunopathological studies indicates a role of gastrointestinal tract associated bacteria in the induction and/or perpetuation of autoimmune diseases [7,27,28,[48][49][50]. Anti-self-Hsp60 antibodies could be induced by pathogenic, e.g., Helicobacter pylori [51][52][53], as well as commensal bacteria like Escherichia coli [47], due to the molecular mimicry.…”

Section: Discussionmentioning

confidence: 99%

“…These antibodies reacted preferentially with Escherichia coli Hsp60 compared with Mycobacterium tuberculosis Hsp65 or human Hsp60. The antibodies to different enterobacterial Hsp60s are suggested to be associated with the inflammatory process and initiation of ankylosing spondylitis (AS) [27,50]. It has been demonstrated that patients with AS (HLA-B27 positive) have high titers of antibodies to the 60 kDa heat shock protein of Klebsiella pneumoniae, the Gram-negative bacteria frequently found in the human gut [49].…”

Section: Discussionmentioning

confidence: 99%

Experimental immunology Human Hsp60 could be a possible target of immune response triggered by Hsp60 of Salmonella Enteritidis – a preliminary study

Dera-Tomaszewska¹,

Krajewska²,

Głośnicka³

2012

cejoi

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Hsp60 of Salmonella Enteritidis appears to be involved in pathogenesis of infectious processes and host immune responses. Because of the similarities between microbial and human Hsps, a humoral response against microbial Hsps may be destructive for the host due to antigen mimicry leading to an autoimmune response. We have performed a preliminary study to investigate whether the homology between Hsp60 of Salmonella Enteritidis and human Hsp60 really exists. ELISA tests were done with success to show that polyclonal antibodies developed against Hsp60 of Salmonella Enteritidis recognize and cross-react with human Hsp60 and one of its seven synthetic peptides used in the study. It was revealed that the antigenic epitopes, which both the proteins have in common, are located between 409 and 424 amino acid residues of human Hsp60 molecule, and are determined by the amino acid sequence of human Hsp60 (409-424) synthetic peptide, the same sequence which was found by other authors to be an immunodominant epitope in patients with acute coronary syndromes. The results show the presence of an immunological and sequence similarity between bacterial Hsp60 and its human counterpart, and suggest that human Hsp60 could be a possible target of immune response triggered by Hsp60 of Salmonella Enteritidis. Salmonella Enteritidis Hsp60 might be potentially involved in autoimmune mechanisms operating in humans. This conclusion must be considered preliminary and hypothesis-generating than hypothesis-proving.

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Infection and Spondyloarthritis

Naovarat¹,

Reveille²

2019

Infections and the Rheumatic Diseases

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Recognition of B cells epitopes of the Klebsiella pneumoniae GroEL-like protein by HLA-B27 positive subjects

Cited by 10 publications

References 27 publications

Klebsiella pneumoniae O antigen loss alters the outer membrane protein composition and the selective packaging of proteins into secreted outer membrane vesicles

Klebsiella pneumoniae O antigen loss alters the outer membrane protein composition and the selective packaging of proteins into secreted outer membrane vesicles

Experimental immunology Human Hsp60 could be a possible target of immune response triggered by Hsp60 of Salmonella Enteritidis – a preliminary study

Infection and Spondyloarthritis

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