ArticlePLoS pathogens2011
Sap transporter mediated import and subsequent degradation of antimicrobial peptides in Haemophilus.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
47 citing papers in PubMed, 87 citations in OpenAlex.
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- PstSCAB and SapBCDF are putrescine exporters inMicrobiology spectrum · 2026Article
- Extracellular defense of bacteria against antimicrobial peptides.Journal of bacteriology · 2025Review
- Rapid identification of key antibiotic resistance genes iniScience · 2025Article
- Structurally diverse C-terminal accessory domains in type I ABC importers reveal distinct regulatory mechanisms.Structure (London, England : 1993) · 2025Review
- Exploiting haem-iron dependence of nontypeableFrontiers in cellular and infection microbiology · 2025Review
- Diverse and specialized metabolic capabilities of microbes in oligotrophic built environments.Microbiome · 2024Article
- Multiple resistance factors collectively promote inoculum-dependent dynamic survival during antimicrobial peptide exposure in Enterobacter cloacae.PLoS pathogens · 2024Article
- Molecular Mechanisms of Bacterial Resistance to Antimicrobial Peptides in the Modern Era: An Updated Review.Microorganisms · 2024Review
- Sensitivity to antimicrobial peptide A (SapA) contributes to the survival of Salmonella typhimurium against antimicrobial peptides, neutrophils and virulence in mice.Archives of microbiology · 2024Article
- Multiple resistance factors collectively promote inoculum-dependent dynamic survival during antimicrobial peptide exposure inbioRxiv : the preprint server for biology · 2024Article
- Antimicrobial Peptide Recognition Motif of the Substrate Binding Protein SapA from NontypeableBiochemistry · 2024Article
- The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria.FEMS microbiology reviews · 2022Review
- Molecular mechanism of SbmA, a promiscuous transporter exploited by antimicrobial peptides.Science advances · 2021Article
- The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions.Chemical Society reviews · 2021Review
- The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent.Antibiotics (Basel, Switzerland) · 2021Review
- The role of antimicrobial peptides in the evolution of endosymbiotic protein import.PLoS pathogens · 2021Article
- The Antibiotic Negamycin Crosses the Bacterial Cytoplasmic Membrane by Multiple Routes.Antimicrobial agents and chemotherapy · 2021Article
- Molecular engineering of antimicrobial peptides: microbial targets, peptide motifs and translation opportunities.Biophysical reviews · 2021Review
- Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Antimicrobial peptides (AMPs) contribute to host innate immune defense and are a critical component to control bacterial infection. Nontypeable Haemophilus influenzae (NTHI) is a commensal inhabitant of the human nasopharyngeal mucosa, yet is commonly associated with opportunistic infections of the upper and lower respiratory tracts. An important aspect of NTHI virulence is the ability to avert bactericidal effects of host-derived antimicrobial peptides (AMPs). The Sap (sensitivity to antimicrobial peptides) ABC transporter equips NTHI to resist AMPs, although the mechanism of this resistance has remained undefined. We previously determined that the periplasmic binding protein SapA bound AMPs and was required for NTHI virulence in vivo. We now demonstrate, by antibody-mediated neutralization of AMP in vivo, that SapA functions to directly counter AMP lethality during NTHI infection. We hypothesized that SapA would deliver AMPs to the Sap inner membrane complex for transport into the bacterial cytoplasm. We observed that AMPs localize to the bacterial cytoplasm of the parental NTHI strain and were susceptible to cytoplasmic peptidase activity. In striking contrast, AMPs accumulated in the periplasm of bacteria lacking a functional Sap permease complex. These data support a mechanism of Sap mediated import of AMPs, a novel strategy to reduce periplasmic and inner membrane accumulation of these host defense peptides.
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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.