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Relationship of Immune Response to Heat-Shock Protein A and Characteristics of Helicobacter pylori -- Infected Patients

1996; Oxford University Press; Volume: 174; Issue: 5 Linguagem: Inglês

10.1093/infdis/174.5.1046

1537-6613

Guillermo I. Pérez‐Pérez, JM Thiberge, A Labigne, Martin J. Blaser,

Toxin Mechanisms and Immunotoxins

Heat-shock protein A (HspA) is a GroES homolog in Helicobacter pylori. Using a recombinant HspA-maltose-binding protein fusion, the serologic response to HspA were determined. For 139 H. pylori-uninfected persons, responses to HspA were low-level or absent. In a survey of 273 infected persons, 105 (38.5%) were seropositive; there was no relationship between clinical outcome of infection and HspA seropositivity. Using paired sera obtained from 39 subjects (mean, 7.1 years apart), the stability of seroresponsiveness to HspA was examined. For 34 persons there was no change in status between the paired sera, but 5 (20%) of 25 initially seronegative persons seroconverted. The hypothesis that HspA seropositivity was related to patient age was examined using sera from 121 asymptomatic H. pylori-infected persons. Both the HspA seropositivity rate and the intensity of the response rose with age. In total, these findings indicate that HspA seropositivity is not universal but may be a consequence of prolonged H. pylori infection.