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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1982-2-25
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pubmed:abstractText |
Strains of Neisseria gonorrhoeae were treated with pyocin 611 131 (pyocin 103) from Pseudomonas aeruginosa PA103, and isogenic resistant variants were isolated. The interaction of pyocin-sensitive and isogenic pyocin-resistant strains with wheat germ agglutinin (WGA) agglutinated all pyocin-sensitive, but not pyocin-resistant, strains. Binding of WGA to three pyocin-sensitive strains and their isogenic pyocin-resistant variants was examined quantitatively by using fluorescein-conjugated lectin. Pyocin-resistant strains maximally bound one-third to one-eighth the quantity of WGA bound by isogenic-sensitive strains. Linear Scatchard plots revealed homogeneous WGA-binding sites on three pyocin-sensitive and one pyocin-resistant strains. Biphasic Scatchard plots, obtained with two pyocin-resistant strains, show that WGA-binding sites in these strains are heterogeneous. The number of WGA-binding sites for pyocin-sensitive organisms ranged from 8 x 10(5) to 1 x 10(6) sites per coccus and from 1 x 10(5) to 3 x 10(5) sites per coccus for pyocin-resistant strains. The apparent association constant for WGA binding to pyocin-sensitive strains ranged from 3 x 10(6) to 6 x 10(6) liters/mol and from 6 x 10(6) to 1 x 10(7) liters/mol for pyocin-resistant strains. Gonococcal lipopolysaccharide was shown to serve as the pyocin 103 receptor by inhibition of pyocin activity. Lipopolysaccharide from a pyocin 103-resistant strain was not able to inhibit pyocin 103 activity. Pyocin 103 resistance was correlated with a structural alteration involving N-acetylglucosamine residues in gonococcal lipopolysaccharide. Based on interactions with wheat germ, soybean, and ricin lectins, a model of lipopolysaccharide structure in N. gonorrhoeae is presented.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-108267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-14047217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-14325874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-237620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-356549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-403141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-405323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-415006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-4208045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-4210728,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-56416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-6155190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-646115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-6775011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-6783533,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-6892800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-6894280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-807676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-809273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-825024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-859000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-92996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6796562-94598
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
148
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
796-803
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
1981
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pubmed:articleTitle |
Interaction with lectins and differential wheat germ agglutinin binding of pyocin 103-sensitive and -resistant Neisseria gonorrhoeae.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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