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Literature summary for 2.3.1.242 extracted from

  • Korneev, K.V.; Kondakova, A.N.; Arbatsky, N.P.; Novototskaya-Vlasova, K.A.; Rivkina, E.M.; Anisimov, A.P.; Kruglov, A.A.; Kuprash, D.V.; Nedospasov, S.A.; Knirel, Y.A.; Drutskaya, M.S.
    Distinct biological activity of lipopolysaccharides with different lipid A acylation status from mutant strains of Yersinia pestis and some members of genus Psychrobacter (2014), Biochemistry (Moscow), 79, 1333-1338.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Yersinia pestis
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Yersinia pestis KM260
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General Information

General Information Comment Organism
physiological function lipid A structures of lpxM and lpxP mutants lack the secondary lauroyl 12:0 group (R3'') or palmitoleoyl 16:1 group (R2''), respectively, and thus both represent a pentaacyl lipid A. Lipid A of Yersinia pestis lpxM/lpxP double mutant lacks both secondary acyl groups, 12:0 and 16:1, and is thus represented by the tetraacyl form. The absence of at least one acyl group is crucial for binding of lipopolysaccharide to toll-like receptor TLR4. Lipopolysaccharide from lpxM and and lpxP mutants induces TNF production at approximately the same level, the former being a slightly stronger activator than the latter Yersinia pestis