Lipopolysaccharide interaction with S2 subunit of pertussis toxin.
作者： M.G. Lei , D.C. Morrison
DOI: 10.1016/S0021-9258(18)54101-6
关键词:
摘要: Abstract Using radioiodinated, photoactivable, reducible cross-linker conjugated bacterial endotoxic lipopolysaccharide (125I-ASD-LPS), we have demonstrated that LPS selectively binds to the S2 subunit of pertussis toxin (PT). Since also interacts with B-oligomer toxin, binding PT is not A-protomer (S1 subunit) dependent. The can be inhibited native underivatized and purified lipid A, suggesting mediated through A moiety molecule. by bovine fetuin glycoprotein. has been interact specifically N-linked oligosaccharide side chains fetuin, interaction may involve carbohydrate-dependent interactions disaccharide backbone S2. Additional studies documented competitively lysozyme but polymyxin B. Sequence analysis allowed identification a high degree amino acid sequence similarity between hen egg white at N-terminal 80-residue regions. Shared lysozyme, PT-S2, third LPS-binding protein alpha-lactalbumin allows tentative second family proteins.
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