Fish soluble Toll-like receptor (TLR)5 amplifies human TLR5 response via physical binding to flagellin.

Abstract:

:Fish has a soluble form of TLR5 ortholog (TLR5S), which does not exist in mammals. We identified TLR5S from rainbow trout and named rtTLR5S, which was about 38% homologous to the extracellular domains of human (hu) and mouse TLR5. Adjuvancy of rtTLR5S to flagellin response by human TLR5 (huTLR5) was tested in this study. A chimera constructed of rtTLR5S and the intracellular TIR of huTLR5 expressed on HeLa cells signaled the presence of various species of bacterial flagellin resulting in NK-kappaB activation. huTLR5S, when co-expressed with rtTLR5S in HeLa cells, augmented response to flagellin resulting in robust huTLR5-mediated NF-kappaB activation. Physical binding of flagellin to rtTLR5S was detected under the conditions where huTLR5 induced rtTLR5S-amplified NF-kappaB activation. Signal amplification by rtTLR5S was specific to huTLR5: no other huTLRs tested were responded to rtTLR5S. These results suggest that the soluble TLR5 serves as an adjuvant augmenting flagellin-TLR5-mediated NF-kappaB activation even in human.

journal_name

Vaccine

journal_title

Vaccine

authors

Tsujita T,Ishii A,Tsukada H,Matsumoto M,Che FS,Seya T

doi

10.1016/j.vaccine.2005.11.003

subject

Has Abstract

pub_date

2006-03-15 00:00:00

pages

2193-9

issue

12

eissn

0264-410X

issn

1873-2518

pii

S0264-410X(05)01126-6

journal_volume

24

pub_type

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