ArticleJournal of bacteriology1997
Molecular characterization and cellular localization of TpLRR, a processed leucine-rich repeat protein of Treponema pallidum, the syphilis spirochete.
Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 30 citations in OpenAlex.
- New insights into the putative role of leucine-rich repeat proteins ofFrontiers in cellular and infection microbiology · 2024Review
- Unusual structural and functional features of TpLRR/BspA-like LRR proteins.Journal of structural biology · 2023Review
- Insight into the Structure, Functions, and Dynamics of theMembranes · 2022Review
- Structural characterization of Treponema pallidum Tp0225 reveals an unexpected leucine-rich repeat architecture.Acta crystallographica. Section F, Structural biology communications · 2019Article
- An extracellular Leptospira interrogans leucine-rich repeat protein binds human E- and VE-cadherins.Cellular microbiology · 2019Article
- Enteric bacteria boost defences against oxidative stress in Entamoeba histolytica.Scientific reports · 2018Article
- Functional insights from proteome-wide structural modeling of Treponema pallidum subspecies pallidum, the causative agent of syphilis.BMC structural biology · 2018Article
- Interaction of Prevotella intermedia strain 17 leucine-rich repeat domain protein AdpF with eukaryotic cells promotes bacterial internalization.Infection and immunity · 2014Article
- Human leucine-rich repeat proteins: a genome-wide bioinformatic categorization and functional analysis in innate immunity.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Reactivity of antibodies from syphilis patients to a protein array representing the Treponema pallidum proteome.Journal of clinical microbiology · 2006Article
- The streptococcal Blr and Slr proteins define a family of surface proteins with leucine-rich repeats: camouflaging by other surface structures.Journal of bacteriology · 2006Article
- Genome scale identification of Treponema pallidum antigens.Infection and immunity · 2005Article
- Characterization of a novel leucine-rich repeat protein antigen from group B streptococci that elicits protective immunity.Infection and immunity · 2005Article
- Multiple functions of the leucine-rich repeat protein LrrA of Treponema denticola.Infection and immunity · 2004Article
- Assessment of the ability to model proteins with leucine-rich repeats in light of the latest structural information.Protein science : a publication of the Protein Society · 2002Article
- Novel 45-kilodalton leptospiral protein that is processed to a 31-kilodalton growth-phase-regulated peripheral membrane protein.Infection and immunity · 2002Article
- Cell adhesion molecules in the pathogenesis of and host defence against microbial infection.Molecular pathology : MP · 1999Review
- Physicochemical evidence that Treponema pallidum TroA is a zinc-containing metalloprotein that lacks porin-like structure.Journal of bacteriology · 1999Article
- Phosphatidylcholine-specific phospholipase C from Listeria monocytogenes is an important virulence factor in murine cerebral listeriosis.Infection and immunity · 1998Article
- Cloning, expression, and sequencing of a cell surface antigen containing a leucine-rich repeat motif from Bacteroides forsythus ATCC 43037.Infection and immunity · 1998Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Automated Edman degradation was used to obtain N-terminal and internal amino acid sequences from a 26-kDa protein in isolated Treponema pallidum outer membranes (OMs). The resulting sequences enabled us to PCR amplify from T. pallidum DNA a 275-bp fragment of the corresponding gene. The complete nucleotide sequence of the gene was determined from fragments amplified by long-distance PCR. Primer extension verified the assigned translational start of the open reading frame (ORF) and putative upstream promoter elements. The ORF encoded a highly basic (pI 9.6) 26-kDa protein which contained an N-terminal 25-amino-acid leader peptide terminated by a signal peptidase I cleavage site. The mature protein contained seven tandemly spaced copies (as well as an eighth incomplete copy) of a leucine-rich repeat (LRR), a motif previously identified in a number of prokaryotic and eukaryotic proteins. Accordingly, the polypeptide was designated T. pallidum leucine-rich repeat protein (TpLRR). Although Triton X-114 phase partitioning showed that TpLRR was hydrophilic, cell localization studies showed that most of the antigen was associated with the peptidoglycan-cytoplasmic membrane complex rather than being freely soluble in the periplasmic space. Immunoblot studies showed that syphilis patients develop a weak antibody response to the antigen. Lastly, the lrr(T. pallidum) gene was mapped to a 60-kb SfiI-SpeI fragment of the T. pallidum chromosome which also contains the rrnA and flaA genes. The function(s) of TpLRR is currently unknown; however, protein-protein and/or protein-lipid interactions mediated by its LRR motifs may facilitate interactions between components of the T. pallidum cell envelope.
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