Abstract
Human enterovirus 71 (EV71) has become the major pathogen of hand, foot, and mouth disease (HFMD) worldwide, while the anti-EV71 antibody responses other than neutralizing epitopes have not been characterized. In this study, EV71 capsid proteins VP1, VP3, VP0 and various VP1 antigens were constructed to analyze anti-EV71 response in severe HFMD cases, non-HFMD outpatient children and normal adults using a novel evolved immunoglobulin-binding molecule (NEIBM)-based ELISA. The high prevalence of antibody responses against all three capsid proteins was demonstrated, and anti-EV71 VP1 showed the main antibody response. Anti-EV71 VP1 antibody response was found to predominantly target to epitopes based on the common enterovirus cross-reactive sequence. Moreover, inhibition pattern against anti-EV71 VP1 reactions in three groups was obviously different. Taken together, these results firstly characterized the anti-EV71 antibody responses which are predominantly against VP1 epitopes based on common enterovirus cross-reactive sequence. This finding could be helpful for the better understanding of anti-EV71 humoral immunity and useful for seroepidemiological surveillance.
Highlights
The host’s innate and adaptive immune responses play key roles in the infection and pathophysiology of viral infections
Anti-enterovirus 71 (EV71) neutralizing antibody detection is currently the only assay to evaluate the seroprevalence of EV71 infection; this analysis does not provide detailed information concerning the characterization of the host antibody response to EV71 infection
We established a novel evolved immunoglobulin-binding molecule (NEIBM)-based enzyme-linked immunoabsorbant assay (ELISA) assay and evaluated the antibody response of various anti-EV71 capsid proteins in severe HFMD cases predominantly infected by EV71 and normal adults as the control group originally to improve anti-EV71 ELISA detection efficacy for the diagnostic purpose
Summary
The host’s innate and adaptive immune responses play key roles in the infection and pathophysiology of viral infections. Studies concerning the host humoral immune responses against EV71 are primarily based on the neutralizing antibody assay. We expressed the EV71 capsid proteins and a series of truncated VP1 proteins to systematically analyze the host antibody response to these proteins and demonstrated that human anti-EV71 antibody responses are predominantly activated in response to VP1, to epitopes based on the common enterovirus cross-reactive sequence. This finding might contribute to a better understanding of anti-EV71 immunity and infection and could be useful for seroepidemiological surveillance and vaccine development
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