{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10"],"submitter":["da Silva RAG"],"funding":["Wellcome Trust","University of Nottingham"],"pubmed_abstract":["Meningococcal lipoprotein, Factor H binding protein (FHbp), is the sole antigen of the Trumenba vaccine (Pfizer) and one of four antigens of the Bexsero vaccine (GSK) targeting <i>Neisseria meningitidis</i> serogroup B isolates. Lipidation of FHbp is assumed to occur for all isolates. We show in the majority of a collection of United Kingdom isolates (1742/1895) non-synonymous single nucleotide polymorphisms (SNPs) in the signal peptide (SP) of FHbp. A single SNP, common to all, alters a polar amino acid that abolishes processing: lipidation and SP cleavage. Whilst some of the FHbp precursor is retained in the cytoplasm due to reduced binding to SecA, remarkably some is translocated and further surface-localized by Slam. Thus we show Slam is not lipoprotein-specific. In a panel of isolates"],"journal":["Frontiers in microbiology"],"pagination":["2847"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6930937"],"repository":["biostudies-literature"],"pubmed_title":["Variant Signal Peptides of Vaccine Antigen, FHbp, Impair Processing Affecting Surface Localization and Antibody-Mediated Killing in Most Meningococcal Isolates."],"pmcid":["PMC6930937"],"pubmed_authors":["Oldfield NJ","Wooldridge KG","Ryan A","Karlyshev AV","Bayliss CD","Griffin R","da Silva RAG"],"additional_accession":[]},"is_claimable":false,"name":"Variant Signal Peptides of Vaccine Antigen, FHbp, Impair Processing Affecting Surface Localization and Antibody-Mediated Killing in Most Meningococcal Isolates.","description":"Meningococcal lipoprotein, Factor H binding protein (FHbp), is the sole antigen of the Trumenba vaccine (Pfizer) and one of four antigens of the Bexsero vaccine (GSK) targeting <i>Neisseria meningitidis</i> serogroup B isolates. Lipidation of FHbp is assumed to occur for all isolates. We show in the majority of a collection of United Kingdom isolates (1742/1895) non-synonymous single nucleotide polymorphisms (SNPs) in the signal peptide (SP) of FHbp. A single SNP, common to all, alters a polar amino acid that abolishes processing: lipidation and SP cleavage. Whilst some of the FHbp precursor is retained in the cytoplasm due to reduced binding to SecA, remarkably some is translocated and further surface-localized by Slam. Thus we show Slam is not lipoprotein-specific. In a panel of isolates","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019","modification":"2026-05-04T09:04:52.714Z","creation":"2020-05-22T10:17:26Z"},"accession":"S-EPMC6930937","cross_references":{"pubmed":["31921030"],"doi":["10.3389/fmicb.2019.02847"]}}