ArticleThe Journal of biological chemistry2012
Hydrolysis of secreted sialoglycoprotein immunoglobulin A (IgA) in ex vivo and biochemical models of bacterial vaginosis.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 85 citations in OpenAlex.
- The cervicovaginal microbiome: an emerging determinant of HPV infection and disease.Journal of virology · 2026Review
- IgA is necessary and sufficient to prevent norovirus infection in mice.Science translational medicine · 2026Article
- Glycan Profile Alterations in Vaginitis and Their Role in Pathogen-Host Interactions.Polish journal of microbiology · 2025Review
- Genetic transformation ofInfection and immunity · 2025Article
- Exploring the vaginal ecosystem: insights into host-microbe interactions and microbial community dynamics.Infection and immunity · 2025Review
- Exploring the role of the vaginal microbiome in HPV infection dynamics: A prospective cohort study.iScience · 2025Article
- Impact of bacterial vaginosis on sexually transmitted viral infections: a bacterial point of view.FEMS microbiology reviews · 2025Review
- Syntrophic bacterial and host-microbe interactions in bacterial vaginosis.The ISME journal · 2025Article
- Vaginal microbiome dysbiosis and sexually transmitted infections correlate with concentrations of immunoglobulin isotypes in human cervicovaginal mucus: insights into HIV-1 transmission.Frontiers in immunology · 2025Article
- IL-33 Participates inJournal of inflammation research · 2025Article
- Article
- Phase variable colony variants are conserved acrossmSphere · 2024Article
- The Sweet Relationship between the Endometrium and Protein Glycosylation.Biomolecules · 2024Review
- IgA coating of vaginal bacteria is reduced in the setting of bacterial vaginosis (BV) and preferentially targets BV-associated species.Infection and immunity · 2024Article
- The role of sialidases in the pathogenesis of bacterial vaginosis and their use as a promising pharmacological target in bacterial vaginosis.Frontiers in cellular and infection microbiology · 2024Review
- Resident microbes shape the vaginal epithelial glycan landscape.Science translational medicine · 2023Article
- Cervicovaginal Gardnerella sialidase-encoding gene in persistent human papillomavirus infection.Scientific reports · 2023Article
- Article
- Dysregulation of immune response in PCOS organ system.Frontiers in immunology · 2023Review
- Protease activities of vaginal Porphyromonas species disrupt coagulation and extracellular matrix in the cervicovaginal niche.NPJ biofilms and microbiomes · 2022Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial vaginosis (BV) is a common polymicrobial imbalance of the vaginal flora associated with a wide variety of obstetric and gynecologic complications including serious infections and preterm birth. As evidenced by high recurrence rates following treatment, interventions for BV are still lacking. Several hydrolytic activities, including glycosidases and proteases, have been previously correlated with BV and have been hypothesized to degrade host sialoglycoproteins that participate in mucosal immune functions. Sialidase activity is most predictive of BV status and correlates strongly with adverse health outcomes. Here we combine clinical specimens with biochemical approaches to investigate secretory immunoglobulin A (SIgA) as a substrate of BV-associated glycosidases and proteases. We show that BV clinical specimens hydrolyze sialic acid from SIgA, but not in the presence of the sialidase inhibitor dehydro-deoxy-sialic acid. The collective action of BV-associated glycosidases exposes underlying mannose residues of SIgA, most apparent on the heavily N-glycosylated secretory component of the antibody. Terminal sialic acid residues on SIgA protect underlying carbohydrate residues from exposure and hydrolysis by exoglycosidases (galactosidase and hexosaminidase). It is known that both IgG and SIgA are present in the human reproductive tract. We show that the IgG heavy chain is more susceptible to proteolysis than its IgA counterpart. Gentle partial deglycosylation of the SIgA secretory component enhanced susceptibility to proteolysis. Together, these data support a model of BV in which SIgA is subject to stepwise exodeglycosylation and enhanced proteolysis, likely compromising the ability of the reproductive mucosa to neutralize and eliminate pathogens.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.