ArticleJournal of bacteriology2009
Group B streptococcus pullulanase crystal structures in the context of a novel strategy for vaccine development.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 31 citations in OpenAlex.
- Biofilm Formation in Streptococcus agalactiae Is Inhibited by a Small Regulatory RNA Regulated by the Two-Component System CiaRH.Microbiology spectrum · 2022Article
- Structural and Functional Analysis of Pullulanase Type 1 (PulA) from Geobacillus thermopakistaniensis.Molecular biotechnology · 2020Article
- Status of group B streptococcal vaccine development.Clinical and experimental vaccine research · 2018Article
- Functional Roles of Starch Binding Domains and Surface Binding Sites in Enzymes Involved in Starch Biosynthesis.Frontiers in plant science · 2018Review
- Review
- Vaccination With a Latch Peptide Provides Serotype-Independent Protection Against Group B Streptococcus Infection in Mice.The Journal of infectious diseases · 2017Article
- Structure and function of α-glucan debranching enzymes.Cellular and molecular life sciences : CMLS · 2016Review
- Enhancing the secretion efficiency and thermostability of a Bacillus deramificans pullulanase mutant (D437H/D503Y) by N-terminal domain truncation.Applied and environmental microbiology · 2015Article
- Identification of genes preferentially expressed by highly virulent piscine Streptococcus agalactiae upon interaction with macrophages.PloS one · 2014Article
- Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Identification of Rgg binding sites in the Streptococcus pyogenes chromosome.Journal of bacteriology · 2011Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The group B streptococcus type I pullulanase (SAP) is a class 13 glycoside hydrolase that is anchored to the bacterial cell surface via a conserved C-terminal anchoring motif and involved in alpha-glucan degradation. Recent in vitro functional studies have shown that SAP is immunogenic in humans and that anti-SAP sera derived from immunized animals impair both group A and group B streptococcus pullulanase activities, suggesting that in vivo immunization with this antigen could prevent streptococcal colonization. To further investigate the putative role of SAP in bacterial pathogenesis, we carried out functional studies and found that recombinant SAP binds to human cervical epithelial cells. Furthermore, with a view of using SAP as a vaccine candidate, we present high-resolution crystal structure analyses of an N-terminally truncated form of SAP lacking the carbohydrate binding module but containing the catalytic domain and displaying glycosidase hydrolase activity, both in its apo form and in complex with maltotetraose, at resolutions of 2.1 and 2.4 A, respectively.
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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.