ArticleInfection and immunity1998
Streptococcal histone-like protein: primary structure of hlpA and protein binding to lipoteichoic acid and epithelial cells.
Article in Infection and immunity, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 62 citations in OpenAlex.
- A modular genetic toolbox for precise gene regulation and multi-color imaging in streptococci.microLife · 2026Article
- Extracellular DNA-protein interactions.Current opinion in structural biology · 2024Review
- Cloning and Functional Analysis of Skin Host Defense Peptides from Yakushima Tago's Brown Frog (Antibiotics (Basel, Switzerland) · 2024Article
- Bacterial nucleoid-associated protein HU as an extracellular player in host-pathogen interaction.Frontiers in cellular and infection microbiology · 2022Review
- Sequence characterisation and novel insights into bovine mastitis-associated Streptococcus uberis in dairy herds.Scientific reports · 2021Article
- Manipulation of the Upper Respiratory Microbiota to Reduce Incidence and Severity of Upper Respiratory Viral Infections: A Literature Review.Frontiers in microbiology · 2021Review
- Expression of an Extracellular Protein (SMU.63) Is Regulated by SprV in Streptococcus mutans.Applied and environmental microbiology · 2020Article
- Antimicrobial Property and Mode of Action of the Skin Peptides of the Sado Wrinkled Frog,Antibiotics (Basel, Switzerland) · 2020Article
- Redirecting the immune response towards immunoprotective domains of a DNABII protein resolves experimental otitis media.NPJ vaccines · 2019Article
- HU ofFrontiers in microbiology · 2018Article
- Monoclonal antibodies against DNA-binding tips of DNABII proteins disrupt biofilms in vitro and induce bacterial clearance in vivo.EBioMedicine · 2016Article
- RNA sequencing uncovers antisense RNAs and novel small RNAs in Streptococcus pyogenes.RNA biology · 2016Article
- Proteomic Investigation of the Response of Enterococcus faecalis V583 when Cultivated in Urine.PloS one · 2015Article
- Distribution and dynamics of epidemic and pandemic Vibrio parahaemolyticus virulence factors.Frontiers in cellular and infection microbiology · 2013Review
- CovR alleviates transcriptional silencing by a nucleoid-associated histone-like protein in Streptococcus mutans.Journal of bacteriology · 2012Article
- Cell surface-associated proteins in the filamentous cyanobacterium Anabaena sp. strain PCC 7120.Microbes and environments · 2012Article
- Genetic and proteomic characterization of rpoB mutations and their effect on nematicidal activity in Photorhabdus luminescens LN2.PloS one · 2012Article
- Post-streptococcal acute glomerulonephritis in children: clinical features and pathogenesis.Pediatric nephrology (Berlin, Germany) · 2011Review
- Surface-exposed histone-like protein a modulates adherence of Streptococcus gallolyticus to colon adenocarcinoma cells.Infection and immunity · 2009Article
- Global dissemination of Vibrio parahaemolyticus serotype O3:K6 and its serovariants.Clinical microbiology reviews · 2007Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
In addition to its role in the nucleoid, the histone-like protein (HlpA) of Streptococcus pyogenes is believed to act as a fortuitous virulence factor in delayed sequelae by binding to heparan sulfate-proteoglycans in the extracellular matrix of target organs and acting as a nidus for in situ immune complex formation. To further characterize this protein, the hlpA genes were cloned from S. pyogenes, S. gordonii, S. mutans, and S. sobrinus, using PCR amplification, and sequenced. The encoded HlpA protein of S. pyogenes has 91 amino acids, a predicted molecular mass of 9,647 Da, an isoelectric point of 9.81, and 90% to 95% sequence identity with HlpA of several oral streptococci. The consensus sequence of streptococcal HlpA has 69% identity with the consensus sequence of the histone-like HB protein of Bacillus species. Oral viridans group streptococci, growing in chemically defined medium at pH 6.8, released HlpA into the milieu during stationary phase as a result of limited cell lysis. HlpA was not released by these bacteria when grown at pH 6.0 or below. S. pyogenes did not release HlpA during growth in vitro; however, analyses of sera from 155 pharyngitis patients revealed a strong correlation (P < 0.0017) between the production of antibodies to HlpA and antibodies to streptolysin O, indicating that the histone-like protein is released by group A streptococci growing in vivo. Extracellular HlpA formed soluble complexes with lipoteichoic acid in vitro and bound readily to heparan sulfate on HEp-2 cell surfaces. These results support a potential role for HlpA in the pathogenesis of streptococcus-induced tissue inflammation.
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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.