Erythrocyte gangliosides act as receptors for Neisseria subflava: identification of the Sia-1 adhesin

Nyberg, G.; Strömberg, Nicklas; Jonsson, Ann‐Beth; Karlsson, Karl‐Anders; Normark, Staffan

doi:10.1128/iai.58.8.2555-2563.1990

Cited by 34 publications

(10 citation statements)

References 30 publications

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“…The adherence of the Opa Ϫ gonococci suggests that adhesins other than Opa mediate the initial close attachment of the gonococci to the microvilli (4,14,36,39,59,74). Several studies have identified lectin-like adhesins other than pili and Opa that bind human glycosphingolipid structures (15,47,50,51,62). Gonococcal adherence to the distal ends of microvilli in the fallopian tube organ culture model was noted previously (20).…”

Section: Discussionmentioning

confidence: 89%

Neisseria gonorrhoeae Coordinately Uses Pili and Opa To Activate HEC-1-B Cell Microvilli, Which Causes Engulfment of the Gonococci

et al. 1999

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This study was undertaken to examine concomitant roles of pili and colony opacity-associated proteins (Opa) in promoting Neisseria gonorrhoeae adherence to and invasion of human endometrial HEC-1-B cells. Adherence of N. gonorrhoeae to cultured HEC-1-B cells was saturable, even though organisms adhered to <50% of the cells. During 4 to 6 h of incubation, adherent mono- and diplococci formed microcolonies on the surfaces of the cells. Microvilli of the HEC-1-B cells adhered by their distal ends to individual cocci within the microcolonies. When the microcolonies grew from isogenic pilus-negative (P−) Opa−, P− Opa+, or P+ Opa−gonococci, microvilli did not elongate, and the colonies were not engulfed. In contrast, the microvilli markedly elongated during exposure to P+ Opa+ gonococci. The microvilli adhered to the organisms along their full lengths and appeared to actively participate in the engulfment of the microcolonies. Internalized microcolonies, with P+ Opa+gonococci, contained dividing cocci and appeared to be surrounded by cell membrane but were not clearly within vacuoles. In contrast, degenerate individual organisms were within vacuoles. Low doses of chloramphenicol, which inhibits protein synthesis by both prokaryotes and eukaryotes, prevented the microvillar response to and internalization of the P+ Opa+ gonococci; higher doses caused internalization without microvillus activation. Cycloheximide and anisomycin, which inhibit only eukaryotic protein synthesis, caused dose-dependent enhancement of uptake. Cytochalasins reduced engulfment; colchicine had no effect. These results show that gonococci must express both pili and Opa to be engulfed efficiently by HEC-1-B cells.

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Section: Discussionmentioning

confidence: 89%

Neisseria gonorrhoeae Coordinately Uses Pili and Opa To Activate HEC-1-B Cell Microvilli, Which Causes Engulfment of the Gonococci

et al. 1999

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“…Our data indicate that the primary site of bacteria-host cell interaction are the host cell microvilli . It would be interesting to test whether the glycolipid receptors for these novel adhesins (42,43), are specifically located at these cell protrusions .…”

Section: Discussionmentioning

confidence: 99%

In situ expression and localization of Neisseria gonorrhoeae opacity proteins in infected epithelial cells: apparent role of Opa proteins in cellular invasion.

Weel

Hopman

Putten

1991

The Journal of Experimental Medicine

109

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SummaryDuring natural infection, gonococcal opacity proteins (Opa) undergo rapid phase variation, but how this phenomenon contributes to the virulence of the bacteria is not well understood. In the present immunomorphological study we examined the actual Opa status ofindividual gonococci during various stages ofgonococcal infection of Chang epithelial cells, by probing ultrathin sections of infected specimens with Opa-specific monoclonal antibodies. Our results demonstrate a heterogeneous Opa expression during the initial interaction of the bacteria, but an almost 100% expression of one of the probed Opas during their secondary attachment and entry into the host cells, suggesting a role for distinct Opas in cellular penetration . The association between Opa expression, tight attachment, and bacterial invasion into the host cells could be confirmed with isogenic variants that expressed different Opa proteins. Once inside the epithelial cells, both morphologically intact, Opa positive and morphologically disintegrated, Opa negative bacteria were observed. The loss ofOpa immiinoreactivity in intracellular gonococci could not be related to the presence of a particular Opa protein, but could be mimicked by incubating the organisms with extracts of sonicated uninfected epithelial cells, suggesting that it was caused by host cell proteolytic activity. Taken together, our data suggest that Opa phase transitions confer a functional adaptation of the bacteria enabling host cell penetration .

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“…Immunogold electron microscopy. Preparation of the samples for the immunogold electron microscopy was done as described by Nyberg et al (26).…”

Section: Ecori Site Of Psup202 By First Digesting the Vector Withmentioning

confidence: 99%

Characterization of a novel chromosomal virulence locus involved in expression of a major surface flagellar sheath antigen of the fish pathogen Vibrio anguillarum

Norqvist

Wolf‐Watz

1993

Infect Immun

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The fish pathogenic bacterium Vibrio anguilarum 775.17B was mutated by the use of transposon Tn5-132. Two hundred independent exconjugants were isolated and screened for a reduction ofvirulence in experimental infections of rainbow trout (Onchorhynchus mykiss). Two of these exconjugants, VAN20 and VAN70, showed a significant reduction in virulence after both intraperitoneal and immersion infections. The avirulent mutants showed no loss of any previously suggested virulence determinants of V. anguillarum. One of the mutants (VAN70) was further characterized. DNA sequence analysis revealed two open reading frames, the gene into which TnS-132 had been inserted (virA) and a closely linked upstream gene (virB). A virB mutant of 775.17B, NQ706, was isolated and also shown to be avirulent. The deduced amino acid sequences of virA and virB correspond to proteins with molecular weights of 36,000 and 42,000, respectively. Insertional mutagenesis of the corresponding virA and virB genes of a clinical isolate of V. anguiUarum, serotype 01, also resulted in avirulence. In immunoblot experiments, the total cell lysates ofVAN70 (virA) and NQ706 (virB) did not respond to a rabbit polyclonal antiserum directed against whole cells of 775.17B (wild type). This suggests that virA and virB are involved in the biosynthesis of a major surface antigen important for the virulence of V. anguillarum. Immunogold electron microscopy showed that a constituent of the flagellar sheath was expressed by 775.17B

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Erythrocyte gangliosides act as receptors for Neisseria subflava: identification of the Sia-1 adhesin

Cited by 34 publications

References 30 publications

Neisseria gonorrhoeae Coordinately Uses Pili and Opa To Activate HEC-1-B Cell Microvilli, Which Causes Engulfment of the Gonococci

Neisseria gonorrhoeae Coordinately Uses Pili and Opa To Activate HEC-1-B Cell Microvilli, Which Causes Engulfment of the Gonococci

In situ expression and localization of Neisseria gonorrhoeae opacity proteins in infected epithelial cells: apparent role of Opa proteins in cellular invasion.

Characterization of a novel chromosomal virulence locus involved in expression of a major surface flagellar sheath antigen of the fish pathogen Vibrio anguillarum

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