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Two mannose-binding lectin homologues and an MBL-associated serine protease are expressed in the gut epithelia of the urochordate species Ciona intestinalis.

Abstract：

:The lectin complement pathway has important functions in vertebrate host defence and accumulating evidence of primordial complement components trace its emergence to invertebrate phyla. We introduce two putative mannose-binding lectin homologues (CioMBLs) from the urochordate species Ciona intestinalis. The CioMBLs display similarities with vertebrate MBLs and comprise a collagen-like region, alpha-helical coiled-coils and a carbohydrate recognition domain (CRD) with conserved residues involved in calcium and carbohydrate binding. Structural analysis revealed an oligomerization through interchain disulphide bridges between N-terminal cysteine residues and cysteines located between the neck region and the CRD. RT-PCR showed a tissue specific expression of CioMBL in the gut and by immunohistochemistry analysis we also demonstrated that CioMBL co-localize with an MBL-associated serine protease in the epithelia cells lining the stomach and intestine. In conclusion we present two urochordate MBLs and identify an associated serine protease, which support the concept of an evolutionary ancient origin of the lectin complement pathway.

journal_name

Dev Comp Immunol

journal_title

Developmental and comparative immunology

authors

Skjoedt MO,Palarasah Y,Rasmussen K,Vitved L,Salomonsen J,Kliem A,Hansen S,Koch C,Skjodt K

doi

10.1016/j.dci.2009.08.004

subject

Has Abstract

pub_date

2010-01-01 00:00:00

pages

59-68

issue

1

eissn

0145-305X

issn

1879-0089

pii

S0145-305X(09)00171-2

journal_volume

34

pub_type

杂志文章

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