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Interactions of Neisseria gonorrhoeae with human neutrophils: studies with purified PII (Opa) outer membrane proteins and synthetic Opa peptides
Journal article   Open access   Peer reviewed

Interactions of Neisseria gonorrhoeae with human neutrophils: studies with purified PII (Opa) outer membrane proteins and synthetic Opa peptides

F L Naids, B Belisle, N Lee and R F Rest
Infection and immunity, v 59(12), pp 4628-4635
Dec 1991
PMID: 1718877
url
https://doi.org/10.1128/iai.59.12.4628-4635.1991View
Published, Version of Record (VoR)Open Access (License Unspecified) Open

Abstract

We investigated the role of gonococcal outer membrane protein PII (also called Opa protein) in nonopsonic adherence to human neutrophils. Gonococcal outer membranes, purified Opa in detergent (Opa), purified Opa in liposomes (Opa+ lips), and peptides composing the second hypervariable (HV2) region of OpaB (strain FA1090) in liposomes (pepHV2 lips) were tested for their abilities to inhibit subsequent gonococcal adherence to human neutrophils. Outer membranes from gonococci possessing adherent Opa, liposomes containing adherent Opa, purified adherent Opa, and two of three liposome preparations (pepHV2 lips) containing peptides from the HV2 region of an adherent Opa inhibited subsequent adherence to neutrophils of homologous Opa+ gonococci. On the other hand, outer membranes from Opa- gonococci, outer membranes containing a nonadherent Opa (OpaA from strain FA1090), purified OpaA, and OpaA lips had little or no inhibitory effect. Outer membranes containing adherent Opas, purified adherent Opas, and liposomes containing such Opas all bound to neutrophils, whereas preparations containing OpaA or no Opa protein did not. The results indicate that (i) Opa proteins can bind to neutrophils in a partially purified or purified form and (ii) the HV2 region of Opa appears to at least partially mediate Opa's biological role.

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Web of Science research areas
Immunology
Infectious Diseases
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