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Sökning: onr:"swepub:oai:lup.lub.lu.se:2eeba551-f7bb-49a0-8d21-eb09c2e1ed66" > Heptose I glycan su...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003559naa a2200385 4500
001oai:lup.lub.lu.se:2eeba551-f7bb-49a0-8d21-eb09c2e1ed66
003SwePub
008160401s2007 | |||||||||||000 ||eng|
0247 a https://lup.lub.lu.se/record/1680672 URI
0247 a https://doi.org/10.1128/IAI.01109-062 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
1001 a Ram, Sanjay4 aut
2451 0a Heptose I glycan substitutions on Neisseria gonorrhoeae lipooligosaccharide influence C4b-binding protein binding and serum resistance.
264 1c 2007
520 a Lipooligosaccharide (LOS) heptose (Hep) glycan substitutions influence gonococcal serum resistance. Several gonococcal strains bind the classical complement pathway inhibitor, C4b-binding protein (C4BP), via their porin (Por) molecule to escape complement-dependent killing by normal human serum (NHS). We show that the proximal glucose (Glc) on HepI is required for C4BP binding to Por1B-bearing gonococcal strains MS11 and 1291 but not to FA19 (Por1A). The presence of only the proximal Glc on HepI (lgtE mutant) permitted maximal C4BP binding to MS11 but not to 1291. Replacing 1291 lgtE Por with MS11 Por increased C4BP binding to levels that paralleled MS11 lgtE, suggesting that replacement of the Por1B molecule dictated the effects of HepI glycans on C4BP binding. The remainder of the strain background did not affect C4BP binding; replacing the Por of strain F62 with MS11 Por (F62 PorMS11) and truncating HepI mirrored the findings in the MS11 background. C4BP binding correlated with resistance to killing by NHS in most instances. F62 PorMS11 and its lgtE mutant were sensitive to NHS despite binding C4BP, secondary to kinetically overwhelming classical pathway activation and possibly increased alternative pathway activation (measured by factor Bb binding) by the F62 background. FA19 lgtF (HepI unsubstituted) resisted killing by only 10% NHS, not 50% NHS, despite binding levels of C4BP similar to those of FA19 and FA19 lgtE (both resistant to 50% serum), suggesting a role for the proximal Glc in serum resistance independently of C4BP binding. This study provides mechanistic insights into how HepI LOS substitutions affect the serum resistance of N. gonorrhoeae.
650 7a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Andra medicinska och farmaceutiska grundvetenskaper0 (SwePub)301992 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Other Basic Medicine0 (SwePub)301992 hsv//eng
7001 a Ngampasutadol, Jutamas4 aut
7001 a Cox, Andrew D4 aut
7001 a Blom, Annau Lund University,Lunds universitet,Proteinkemi, Malmö,Forskargrupper vid Lunds universitet,Protein Chemistry, Malmö,Lund University Research Groups4 aut0 (Swepub:lu)klke-abl
7001 a Lewis, Lisa A4 aut
7001 a St Michael, Frank4 aut
7001 a Stupak, Jacek4 aut
7001 a Gulati, Sunita4 aut
7001 a Rice, Peter A4 aut
7102 a Proteinkemi, Malmöb Forskargrupper vid Lunds universitet4 org
7730 t Infection and Immunityg 75:8, s. 4071-4081q 75:8<4071-4081x 1098-5522
8564 u http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17526744&dopt=Abstractx freey FULLTEXT
8564 u http://dx.doi.org/10.1128/IAI.01109-06x freey FULLTEXT
8564 8u https://lup.lub.lu.se/record/168067
8564 8u https://doi.org/10.1128/IAI.01109-06

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