ArticleInfection and immunity2002
Autotransported serine protease A of Neisseria meningitidis: an immunogenic, surface-exposed outer membrane, and secreted protein.
Article in Infection and immunity, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 71 citations in OpenAlex.
- Identification of an autotransporter peptidase of Rickettsia rickettsii responsible for maturation of surface exposed autotransporters.PLoS pathogens · 2023Article
- Multilayer Regulation ofMicroorganisms · 2022Article
- Phylogenetic survey of the subtilase family and a data-mining-based search for new subtilisins fromFrontiers in microbiology · 2022Article
- The Serine Protease Autotransporters TagB, TagC, and Sha from Extraintestinal PathogenicInternational journal of molecular sciences · 2020Article
- Article
- Biological Functions of the Secretome ofFrontiers in cellular and infection microbiology · 2017Review
- Interstrain Cooperation in Meningococcal Biofilms: Role of Autotransporters NalP and AutA.Frontiers in microbiology · 2017Article
- Characterization and Distribution of theFrontiers in cellular and infection microbiology · 2017Article
- Expression of the Gene for Autotransporter AutB ofFrontiers in cellular and infection microbiology · 2016Article
- Nuclear trafficking, histone cleavage and induction of apoptosis by the meningococcal App and MspA autotransporters.Cellular microbiology · 2015Article
- Structure and protective efficacy of the Staphylococcus aureus autocleaving protease EpiP.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Neisseria meningitidis NalP cleaves human complement C3, facilitating degradation of C3b and survival in human serum.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Transcriptional profiling of Neisseria meningitidis interacting with human epithelial cells in a long-term in vitro colonization model.Infection and immunity · 2013Article
- Article
- From self sufficiency to dependence: mechanisms and factors important for autotransporter biogenesis.Nature reviews. Microbiology · 2012Review
- The AprV5 subtilase is required for the optimal processing of all three extracellular serine proteases from Dichelobacter nodosus.PloS one · 2012Article
- Asparagine peptide lyases: a seventh catalytic type of proteolytic enzymes.The Journal of biological chemistry · 2011Article
- Genotypic and phenotypic modifications of Neisseria meningitidis after an accidental human passage.PloS one · 2011Article
- Comparative analysis of the biochemical and functional properties of C-terminal domains of autotransporters.Journal of bacteriology · 2010Article
- Comparative genome biology of a serogroup B carriage and disease strain supports a polygenic nature of meningococcal virulence.Journal of bacteriology · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several autotransporter proteins have previously been identified in Neisseria meningitidis. Using molecular features common to most members of the autotransporter family of proteins, we have identified an additional novel ca. 112-kDa autotransporter protein in the meningococcal genomic sequence data. This protein, designated autotransported serine protease A (AspA), has significant N-terminal homology to the secreted serine proteases (subtilases) from several organisms and contains a serine protease catalytic triad. The amino acid sequence of AspA is well-conserved in serogroup A, B, and C meningococci. In Neisseria gonorrhoeae, the AspA homologue appears to be a pseudogene. The gene encoding AspA was cloned and expressed from meningococcal strain MC58 (B15:P1.16b). Anti-AspA antibodies were detected in patients' convalescent-phase sera, suggesting that AspA is expressed in vivo during infection and is immunogenic and cross-reactive. Rabbit polyclonal monospecific anti-AspA serum was used to probe whole-cell proteins from a panel of wild-type meningococcal strains and two AspA mutant strains. Expression of the ca. 112-kDa precursor polypeptide was detected in 12 of 20 wild-type meningococcal strains examined, suggesting that AspA expression is phase variable. Immunogold electron microscopy and cellular fractionation studies showed that the AspA precursor is transported to the outer membrane and remains surface exposed. Western blot experiments confirmed that smaller, ca. 68- or 70-kDa components of AspA (AspA68 and AspA70, respectively) are then secreted into the meningococcal culture supernatant. Site-directed mutagenesis of S426 abolished secretion of both rAspA68 and rAspA70 in Escherichia coli, confirming that AspA is an autocleaved autotransporter protein. In conclusion, we characterized a novel, surface-exposed and secreted, immunogenic, meningococcal autotransporter protein.
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