ArticleNature microbiology2016
Slam is an outer membrane protein that is required for the surface display of lipidated virulence factors in Neisseria.
Article in Nature microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 75 citations in OpenAlex.
- Evaluation of the surface lipoprotein assembly modifier (Slam) as a vaccine candidate against Neisseria gonorrhoeae infection.Scientific reports · 2026Article
- Structure-based engineering of a nutrient acquisition protein enhances neutralizing antibodies and protection for the development of a gonococcal vaccine.bioRxiv : the preprint server for biology · 2025Article
- Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota.Nature microbiology · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- Surface lipoprotein sorting by crosstalk between Lpt and Lol pathways in gram-negative bacteria.Nature communications · 2025Article
- A surface lipoprotein on Pasteurella multocida binds complement factor I to promote immune evasion.PLoS pathogens · 2025Article
- Bioinformatic discovery of type 11 secretion system (T11SS) cargo across theMicrobial genomics · 2025Article
- Characterizing host-microbe interactions with bacterial effector proteins using proximity-dependent biotin identification (BioID).Communications biology · 2025Review
- Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs.Scientific reports · 2024Article
- Bacterial hemophilin homologs and their specific type eleven secretor proteins have conserved roles in heme capture and are diversifying as a family.Journal of bacteriology · 2024Article
- Prevalence of Slam-dependent hemophilins in Gram-negative bacteria.Journal of bacteriology · 2024Article
- DeepSS2GO: protein function prediction from secondary structure.Briefings in bioinformatics · 2024Article
- Examining Protein Translocation by β-Barrel Membrane Proteins Using Reconstituted Proteoliposomes.Methods in molecular biology (Clifton, N.J.) · 2024Article
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- Structural and functional insights into iron acquisition from lactoferrin and transferrin in Gram-negative bacterial pathogens.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Article
- A Borrelia burgdorferi LptD homolog is required for flipping of surface lipoproteins through the spirochetal outer membrane.Molecular microbiology · 2023Article
- Reverse vaccinology-based identification of a novel surface lipoprotein that is an effective vaccine antigen against bovine infections caused by Pasteurella multocida.PLoS pathogens · 2023Article
- Unmasking of the von Willebrand A-domain surface adhesin CglB at bacterial focal adhesions mediates myxobacterial gliding motility.Science advances · 2023Article
- Neisseria genes required for persistence identified via in vivo screening of a transposon mutant library.PLoS pathogens · 2022Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipoproteins decorate the surface of many Gram-negative bacterial pathogens, playing essential roles in immune evasion and nutrient acquisition. In Neisseria spp., the causative agents of gonorrhoea and meningococcal meningitis, surface lipoproteins (SLPs) are required for virulence and have been extensively studied as prime candidates for vaccine development. However, the machinery and mechanism that allow for the surface display of SLPs are not known. Here, we describe a transposon (Tn5)-based search for the proteins required to deliver SLPs to the surface of Neisseria meningitidis, revealing a family of proteins that we have named the surface lipoprotein assembly modulator (Slam). N. meningitidis contains two Slam proteins, each exhibiting distinct substrate preferences. The Slam proteins are sufficient to reconstitute SLP transport in laboratory strains of Escherichia coli, which are otherwise unable to efficiently display these lipoproteins on their cell surface. Immunoprecipitation and domain probing experiments suggest that the SLP, TbpB, interacts with Slam during the transit process; furthermore, the membrane domain of Slam is sufficient for selectivity and proper surface display of SLPs. Rather than being a Neisseria-specific factor, our bioinformatic analysis shows that Slam can be found throughout proteobacterial genomes, indicating a conserved but until now unrecognized virulence mechanism.
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