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Binding of porcine ficolin-alpha to lipopolysaccharides from Gram-negative bacteria and lipoteichoic acids from Gram-positive bacteria.

Abstract：

:Protein(s) reactive with N-acetyl-D-glucosamine (GlcNAc) was isolated from porcine nonimmune serum. The molecular weight of the purified protein was found to be mainly 40 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions. The N-terminal 10 amino acid sequence of the purified protein were found to be identical to that of porcine ficolin-alpha reported previously. In enzyme-linked immunosorbent assay, the purified protein was found to react with lipopolysaccharides (LPS) from different Gram-negative bacteria such as Esherichia coli, Salmonella typhimurium, Salmonella enteritidis, Salmonella abortus equi, Pseudomonas aeruginosa, Shigella flexeneri, and Serratia marcescens and with lipoteichoic acid (LTA) from Gram-positive bacteria such as Streptococcus sanguis, Bacillus subtilis, Streptococcus pyogenes, and Staphylococcus aureus. The purified protein also reacted with E. coli O26 isolated from food poisoning and bovine feces and heat-treated Gram-positive bacteria such as S. aureus, B. cereus, B. subtilis, Enterococcus faecium, and Corynebacterum bovis. On the other hand, porcine IgG isolated from nonimmune serum showed different reactivity with these LPS, LTA, and heat-treated bacterial cells. From the present findings, purified porcine serum protein reactive with GlcNAc is concluded to be ficolin-alpha playing an important role(s) in innate immunity against microbial infection with Gram-positive and -negative bacteria.

journal_name

Dev Comp Immunol

journal_title

Developmental and comparative immunology

authors

Nahid AM,Sugii S

doi

10.1016/j.dci.2005.04.002

keywords:

subject

Has Abstract

pub_date

2006-01-01 00:00:00

pages

335-43

issue

3

eissn

0145-305X

issn

1879-0089

pii

S0145-305X(05)00085-6

journal_volume

30

pub_type

杂志文章

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