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PMID: 1679039 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Pseudomonas aeruginosa exoenzyme S is an adhesion.

Infection and immunity ·Vol. 59 ·No. 9 ·1991-09-00 ·Pages 2859-63

Baker NR, Minor V, Deal C, Shahrabadi MS, Simpson DA, Woods DE

Abstract

Exoenzyme S from Pseudomonas aeruginosa has been studied as an adhesion for glycosphingolipids and buccal cells. Binding of exoenzyme S to gangliotriosylceramide (GalNAc beta 1-4Gal beta 1-4Glc beta 1-1Cer), gangliotetraosylceramide (Gal beta 1-3 GalNAcT beta 1-4 Gal beta 1-4Glc beta 1-1Cer), and lactosylceramide (Gal beta 1-4Glc beta 1-1Cer) separated on thin-layer chromatograms was observed. Binding curves for exoenzyme S with dilutions of gangliotetraosylceramide immobilized on plastic plates were similar to previously reported results for the intact bacteria. Binding of exoenzyme S to sialylated counterparts of these glycosphingolipids was not seen, indicating that the addition of a sialic acid residue interferes with binding. Exoenzyme S and monoclonal antibody to exoenzyme S inhibit the binding of P. aeruginosa to buccal cells. The presence of exoenzyme S on the surface of P. aeruginosa was detected by immunogold labeling of bacteria with antibodies to exoenzyme S. Results of these studies led us to conclude that exoenzyme S is an important adhesion of P. aeruginosa.

MeSH Terms
ADP Ribose Transferases Adhesins, Bacterial Animals Antigens, CD Bacterial Adhesion/immunology Bacterial Proteins/metabolism Bacterial Toxins Carbohydrate Sequence Fimbriae, Bacterial/metabolism Gangliosides Glycosphingolipids/metabolism Immunohistochemistry Lactosylceramides Lectins Molecular Sequence Data Poly(ADP-ribose) Polymerases/immunology,metabolism Pseudomonas aeruginosa/enzymology,immunology,ultrastructure Rabbits
Chemicals
Adhesins, Bacterial Antigens, CD Bacterial Proteins Bacterial Toxins G(A1) ganglioside Gangliosides Glycosphingolipids Lactosylceramides Lectins adhesin, Pseudomonas ganglio-N-triaosylceramide CDw17 antigen ADP Ribose Transferases Poly(ADP-ribose) Polymerases exoenzyme S
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Baker N R
Department of Microbiology, Ohio State University, Columbus 43210.
Minor V
Deal C
Shahrabadi M S
Simpson D A
Woods D E
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
DOI
10.1128/iai.59.9.2859-2863.1991
Published
1991-09-00
Pages
2859-63
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC258105
Subset
IM
External Links
PubMed source DOI: 10.1128/iai.59.9.2859-2863.1991 PMC Full Text View journal details
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