<i>Helicobacter pylori</i> secretes the chaperonin GroEL (HSP60), which binds iron

González-López, Marco A.; Velázquez-Guadarrama, Norma; Romero-Espejel, María Elena; Olivares-Trejo, José de Jesús

doi:10.1016/j.febslet.2013.04.048

Cited by 31 publications

(26 citation statements)

References 23 publications

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“…Candidate vaccine studies in rodents have demonstrated that anti‐Catalase antibodies protect against H. pylori infection . The molecular chaperone GroEL is required for the proper folding of extracellular proteins and also binds iron, an essential element for the bacterial infective process …”

Section: Discussionmentioning

confidence: 99%

Serological response to Helicobacter pylori infection among Latin American populations with contrasting risks of gastric cancer

Camargo

Beltrán

Conde-Glez

et al. 2015

Intl Journal of Cancer

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Gastric cancer is a rare outcome of chronic Helicobacter pylori infection. Serologic profiles may reveal bacterial, environmental and/or host factors associated with cancer risk. We therefore compared specific anti-H. pylori antibodies among populations with at least 2-fold differences in gastric cancer mortality from Mexico, Colombia and Chile. Our study included 1,776 adults (mean age 42 years) from three nationally representative surveys, equally divided between residents of high- and low-risk areas. Antibodies to 15 immunogenic H. pylori antigens were measured by fluorescent bead-based multiplex assays; results were summarized to identify overall H. pylori seropositivity. We used logistic regression to model associations between antibody seroreactivity and regional cancer risk (high vs. low), adjusting for country, age and sex. Both risk areas had similar H. pylori seroprevalence. Residents in high- and low-risk areas were seroreactive to a similar number of antigens (means 8.2 vs. 7.9, respectively; adjusted-odds ratio, OR: 1.02, p=0.05). Seroreactivities to Catalase and the known virulence proteins CagA and VacA were each significantly (p<0.05) associated with residence in high-risk areas, but ORs were moderate (1.26, 1.42, and 1.41, respectively) and their discriminatory power was low (ROC area under curve <0.6). The association of Catalase was independent from effects of either CagA or VacA. Sensitivity analyses for antibody associations restricted to H. pylori-seropositive individuals generally replicated significant associations. Our findings suggest that humoral responses to H. pylori are insufficient to distinguish high and low gastric cancer risk in Latin America. Factors determining population variation of gastric cancer burden remain to be identified.

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Section: Discussionmentioning

confidence: 99%

Serological response to Helicobacter pylori infection among Latin American populations with contrasting risks of gastric cancer

Camargo

Beltrán

Conde-Glez

et al. 2015

Intl Journal of Cancer

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“…Interestingly, the co‐chaperonin XnGroES was not found in the OMVs, suggesting a specific export pathway for XnGroEL. How XnGroEL is secreted is not known, but GroEL secretion was previously observed in other bacteria including Helicobacter pylori and Bacillus subtilis (Yang et al ., ; Gonzales‐Lopez et al ., ). The purified XnGroEL was insecticidal to larvae of the cotton bollworm Helicoverpa armigera after oral administration (Joshi et al ., ).…”

Section: Groel As An Important Virulence Factor Of Entomopathogenic Bmentioning

confidence: 97%

Versatile roles of the chaperonin GroEL in microorganism-insect interactions

Kupper

Gupta

Feldhaar³

et al. 2014

FEMS Microbiol Lett

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The chaperonin 60 (Cpn60) is present in all three kingdoms of life and is one of the most conserved proteins in living organisms. The Escherichia coli Cpn60 (GroEL) is the best studied representative of the huge Cpn60 family. It is an essential protein because in conjunction with the chaperonin 10 (Cpn10 or GroES) it forms a protein-folding machine required for correct folding of many proteins and for recycling of misfolded proteins. As many other chaperones, GroEL and GroES are also known as heat-shock proteins (HSPs), since heat stress leads to a strong induction of their expression, a measure to counteract the increase in misfolded proteins as a result of a high nonphysiological temperature. A large amount of literature is available which is dedicated to the elucidation of how protein folding is assisted by this molecular chaperone. However, apart from this primary task, additional so-called 'moonlighting' functions of GroEL proteins unrelated to their folding activity have emerged in the past years. In fact, it becomes apparent that GroEL proteins have diverse functions in particular in mutualistic and pathogenic microorganism-host interactions. In this brief review, we describe some of these recent findings focusing on the importance of GroEL for microorganism-insect interactions.

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“…Antibody responses against hsp60 Hp (Gonzalez-Lopez et al, 2013) were tested by western immunoblotting, as previously described with slight modifications (Bogdanos et al, 2004, Koutsoumpas et al, 2009 …”

Section: Anti-hsp60 Hp Antibody Testing By Immunoblottingmentioning

confidence: 99%

“…Antibody responses to Hp-specific hsp60 (Gonzalez-Lopez et al, 2013) has not been studied in great detail in MS. In the present study, we assessed such antibody reactivities in patients with RRMS and SPMS.…”

Section: Introductionmentioning

confidence: 99%