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'''Vaginolysin''' ('''VLY''') is a toxin produced by ''Gardnerella'' ''vaginalis'', a bacterium commonly associated with bacterial vaginosis.<ref>{{Cite journal |last=Gelber |first=Shari E. |last2=Aguilar |first2=Jorge L. |last3=Lewis |first3=Kanako L. T. |last4=Ratner |first4=Adam J. |date=2008 |title=Functional and Phylogenetic Characterization of Vaginolysin, the Human-Specific Cytolysin from Gardnerella vaginalis |url=https://journals.asm.org/doi/10.1128/jb.01965-07 |journal=Journal of Bacteriology |volume=190 |issue=11 |pages=3896–3903 |doi=10.1128/jb.01965-07 |pmc=PMC2395025 |pmid=18390664}}</ref> VLY is a member of the cholesterol-dependent cytolysin family, characterized by their ability to form pores in cholesterol rich membranes. The most closely related protein is intermedilysin'','' which is produced by ''Streptococcus intermedius''.<ref>{{Cite journal |last=Caza |first=Mélissa |last2=Kronstad |first2=James W. |date=2013 |title=Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans |url=http://journal.frontiersin.org/article/10.3389/fcimb.2013.00080/abstract |journal=Frontiers in Cellular and Infection Microbiology |volume=3 |doi=10.3389/fcimb.2013.00080 |issn=2235-2988}}</ref> '''Vaginolysin''' ('''VLY''') is a toxin produced by ], a bacterium commonly associated with bacterial vaginosis.<ref>{{Cite journal |last=Gelber |first=Shari E. |last2=Aguilar |first2=Jorge L. |last3=Lewis |first3=Kanako L. T. |last4=Ratner |first4=Adam J. |date=2008 |title=Functional and Phylogenetic Characterization of Vaginolysin, the Human-Specific Cytolysin from Gardnerella vaginalis |url=https://journals.asm.org/doi/10.1128/jb.01965-07 |journal=Journal of Bacteriology |volume=190 |issue=11 |pages=3896–3903 |doi=10.1128/jb.01965-07 |pmc=PMC2395025 |pmid=18390664}}</ref> VLY is a member of the cholesterol-dependent cytolysin family, characterized by their ability to form pores in cholesterol rich membranes. The most closely related protein is intermedilysin'','' which is produced by ''Streptococcus intermedius''.<ref>{{Cite journal |last=Caza |first=Mélissa |last2=Kronstad |first2=James W. |date=2013 |title=Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans |url=http://journal.frontiersin.org/article/10.3389/fcimb.2013.00080/abstract |journal=Frontiers in Cellular and Infection Microbiology |volume=3 |doi=10.3389/fcimb.2013.00080 |issn=2235-2988}}</ref>


VLY exhibits cytolytic activity against human erythrocytes, causing lysis of red blood cells. This process releases iron, an essential bnutrient for microbial pathogens. In vitro studies have also demonstrated VLY induces membrane blebbing in human vaginal and cervical cells, suggesting its role in epithelial cell damage.<ref>{{Cite journal |last=Randis |first=Tara M. |last2=Zaklama |first2=Joanne |last3=LaRocca |first3=Timothy J. |last4=Los |first4=Ferdinand C. O. |last5=Lewis |first5=Emma L. |last6=Desai |first6=Purnahamsi |last7=Rampersaud |first7=Ryan |last8=Amaral |first8=Fábio E. |last9=Ratner |first9=Adam J. |date=2013 |title=Vaginolysin Drives Epithelial Ultrastructural Responses to Gardnerella vaginalis |url=https://journals.asm.org/doi/10.1128/iai.00627-13 |journal=Infection and Immunity |volume=81 |issue=12 |pages=4544–4550 |doi=10.1128/iai.00627-13 |pmc=PMC3837968 |pmid=24082080}}</ref> VLY exhibits cytolytic activity against human erythrocytes, causing lysis of ]. This process releases iron, an essential bnutrient for microbial pathogens. In vitro studies have also demonstrated VLY induces membrane blebbing in human vaginal and cervical cells, suggesting its role in epithelial cell damage.<ref>{{Cite journal |last=Randis |first=Tara M. |last2=Zaklama |first2=Joanne |last3=LaRocca |first3=Timothy J. |last4=Los |first4=Ferdinand C. O. |last5=Lewis |first5=Emma L. |last6=Desai |first6=Purnahamsi |last7=Rampersaud |first7=Ryan |last8=Amaral |first8=Fábio E. |last9=Ratner |first9=Adam J. |date=2013 |title=Vaginolysin Drives Epithelial Ultrastructural Responses to Gardnerella vaginalis |url=https://journals.asm.org/doi/10.1128/iai.00627-13 |journal=Infection and Immunity |volume=81 |issue=12 |pages=4544–4550 |doi=10.1128/iai.00627-13 |pmc=PMC3837968 |pmid=24082080}}</ref>


The cytolytic activities of VLY are hypothesized to contribute to the virulence of''Neisseria gonorrhoeae'', potentially by facilitating the bacterium's access to intracellular metabolites and aiding in its evasion of host immune responses.<ref>{{Cite journal |last=Morrill |first=Sydney R |last2=Saha |first2=Sudeshna |last3=Varki |first3=Ajit P |last4=Lewis |first4=Warren G |last5=Ram |first5=Sanjay |last6=Lewis |first6=Amanda L |date=2023 |title=Gardnerella Vaginolysin Potentiates Glycan Molecular Mimicry by Neisseria gonorrhoeae |url=https://academic.oup.com/jid/article/228/11/1610/7276580 |journal=The Journal of Infectious Diseases |volume=228 |issue=11 |pages=1610–1620 |doi=10.1093/infdis/jiad391 |issn=0022-1899 |pmc=PMC10681867 |pmid=37722688}}</ref> The cytolytic activities of VLY are hypothesized to contribute to the virulence of '']'', potentially by facilitating the bacterium's access to intracellular metabolites and aiding in its evasion of host immune responses.<ref>{{Cite journal |last=Morrill |first=Sydney R |last2=Saha |first2=Sudeshna |last3=Varki |first3=Ajit P |last4=Lewis |first4=Warren G |last5=Ram |first5=Sanjay |last6=Lewis |first6=Amanda L |date=2023 |title=Gardnerella Vaginolysin Potentiates Glycan Molecular Mimicry by Neisseria gonorrhoeae |url=https://academic.oup.com/jid/article/228/11/1610/7276580 |journal=The Journal of Infectious Diseases |volume=228 |issue=11 |pages=1610–1620 |doi=10.1093/infdis/jiad391 |issn=0022-1899 |pmc=PMC10681867 |pmid=37722688}}</ref>




Revision as of 17:32, 22 January 2025

Vaginolysin (VLY) is a toxin produced by Gardnerella vaginalis, a bacterium commonly associated with bacterial vaginosis. VLY is a member of the cholesterol-dependent cytolysin family, characterized by their ability to form pores in cholesterol rich membranes. The most closely related protein is intermedilysin, which is produced by Streptococcus intermedius.

VLY exhibits cytolytic activity against human erythrocytes, causing lysis of red blood cells. This process releases iron, an essential bnutrient for microbial pathogens. In vitro studies have also demonstrated VLY induces membrane blebbing in human vaginal and cervical cells, suggesting its role in epithelial cell damage.

The cytolytic activities of VLY are hypothesized to contribute to the virulence of Neisseria gonorrhoeae, potentially by facilitating the bacterium's access to intracellular metabolites and aiding in its evasion of host immune responses.



References

  1. Gelber, Shari E.; Aguilar, Jorge L.; Lewis, Kanako L. T.; Ratner, Adam J. (2008). "Functional and Phylogenetic Characterization of Vaginolysin, the Human-Specific Cytolysin from Gardnerella vaginalis". Journal of Bacteriology. 190 (11): 3896–3903. doi:10.1128/jb.01965-07. PMC 2395025. PMID 18390664.{{cite journal}}: CS1 maint: PMC format (link)
  2. Caza, Mélissa; Kronstad, James W. (2013). "Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans". Frontiers in Cellular and Infection Microbiology. 3. doi:10.3389/fcimb.2013.00080. ISSN 2235-2988.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  3. Randis, Tara M.; Zaklama, Joanne; LaRocca, Timothy J.; Los, Ferdinand C. O.; Lewis, Emma L.; Desai, Purnahamsi; Rampersaud, Ryan; Amaral, Fábio E.; Ratner, Adam J. (2013). "Vaginolysin Drives Epithelial Ultrastructural Responses to Gardnerella vaginalis". Infection and Immunity. 81 (12): 4544–4550. doi:10.1128/iai.00627-13. PMC 3837968. PMID 24082080.{{cite journal}}: CS1 maint: PMC format (link)
  4. Morrill, Sydney R; Saha, Sudeshna; Varki, Ajit P; Lewis, Warren G; Ram, Sanjay; Lewis, Amanda L (2023). "Gardnerella Vaginolysin Potentiates Glycan Molecular Mimicry by Neisseria gonorrhoeae". The Journal of Infectious Diseases. 228 (11): 1610–1620. doi:10.1093/infdis/jiad391. ISSN 0022-1899. PMC 10681867. PMID 37722688.{{cite journal}}: CS1 maint: PMC format (link)
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