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. 1989 Jun;57(6):1691–1696. doi: 10.1128/iai.57.6.1691-1696.1989

Heterogeneity of the L-rhamnose residue in the outer core of Pseudomonas aeruginosa lipopolysaccharide, characterized by using human monoclonal antibodies.

S Yokota 1, H Ochi 1, H Ohtsuka 1, M Kato 1, H Noguchi 1
PMCID: PMC313341  PMID: 2498204

Abstract

Hybridoma cell lines producing human monoclonal antibodies (MAbs) MH-4H7 and KN-2B11 [immunoglobulin M (lambda)] which bound to the outer core region of Pseudomonas aeruginosa lipopolysaccharide (LPS) were established by cell fusion of human peripheral lymphocytes with human-mouse heteromyeloma SHM D-33. Both binding specificity experiments with a series of LPS-defective mutants derived from P. aeruginosa PAC1R (P. S. N. Rowe and P. M. Meadow, Eur. J. Biochem.132:329-337, 1983) and competitive enzyme immunoassay experiments with monosaccharides demonstrated that alpha-L-rhamnose residues in the outer core of LPS might be in part an epitope. The MAbs specifically bound to clinical isolates belonging to Homma serotypes A, F, G, and K at a frequency of 70 to 86% and to serotypes H and M isolates at about 50%. They did not bind to any isolates of serotype B, E, and I tested. This evidence indicates that L-rhamnose and probably its neighboring residues in the other core of P. aeruginosa are heterogeneous in some association with the O serotype.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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