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The outer membrane protein X from Escherichia coli exhibits immune properties.

Abstract：

:Outer membrane proteins (OMP) are expressed in Gram-negative bacterial cell wall. OmpA from Klebsiella pneumoniae (KpOmpA) has been shown to bind and to activate selectively antigen presenting cells (APCs), eliciting protective CTL responses. In this study, we investigated whether OmpX, another member of the OMP family and structurally related to OmpA, exhibits the same immune properties. Using recombinant OmpX from Escherichia coli (EcOmpX), we report that EcOmpX binds to and is internalized by human APCs. However, EcOmpX does not activate APCs. EcOmpX acts as an efficient carrier protein as it induces a potent and Th1/Th2 mixed anti-TNP humoral response. However, adjuvant is required to generate a protective anti-tumoral immune response in mice injected with a tumor model antigen coupled to EcOmpX. Collectively, these data show that EcOmpX is recognized by innate cells but does not activate them, suggesting that EcOmpX does not provide a signal danger to APCs. In conclusion, this study provides information on the molecular mechanisms involved in the recognition and activation of innate cells by bacterial outer membrane proteins.

journal_name

Vaccine

journal_title

Vaccine

authors

Maisnier-Patin K,Malissard M,Jeannin P,Haeuw JF,Corbière JC,Hoeffel G,Gauchat JF,Nguyen T,Saez JM,Delneste Y

doi

10.1016/s0264-410x(03)00316-5

subject

Has Abstract

pub_date

2003-09-08 00:00:00

pages

3765-74

issue

25-26

eissn

0264-410X

issn

1873-2518

pii

S0264410X03003165

journal_volume

21

pub_type

杂志文章

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