ArticleThe Journal of biological chemistry2011
Molecular characterization of the interaction between sialylated Neisseria gonorrhoeae and factor H.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 39 citations in OpenAlex.
- Review
- Bacterial post-translational changes: the possible enigma of multidrug resistance.Archives of microbiology · 2026Review
- Discovery and characterization of vertebrate sialoglycan-binding proteins.Seminars in immunology · 2025Review
- Identification of a Kingella kingae factor H binding protein that is the major determinant of serum resistance.PLoS pathogens · 2025Article
- Terminal complement complexes with or without C9 potentiate antimicrobial activity againstmBio · 2025Article
- Rational selection of TbpB variants yields a bivalent vaccine with broad coverage against Neisseria gonorrhoeae.NPJ vaccines · 2025Article
- Gardnerella Vaginolysin Potentiates Glycan Molecular Mimicry by Neisseria gonorrhoeae.The Journal of infectious diseases · 2023Article
- Bacterium of one thousand and one variants: genetic diversity ofMicrobial genomics · 2023Review
- An optimized Factor H-Fc fusion protein against multidrug-resistantFrontiers in immunology · 2022Article
- Interactions Between PathogenicFrontiers in cellular and infection microbiology · 2021Review
- Hijacking Factor H for Complement Immune Evasion.Frontiers in immunology · 2021Review
- Development of Complement Factor H-Based Immunotherapeutic Molecules in Tobacco Plants Against Multidrug-ResistantFrontiers in immunology · 2020Article
- Human Factor H Domains 6 and 7 Fused to IgG1 Fc Are Immunotherapeutic againstJournal of immunology (Baltimore, Md. : 1950) · 2018Article
- Complement factor H in host defense and immune evasion.Cellular and molecular life sciences : CMLS · 2017Review
- Utilizing complement evasion strategies to design complement-based antibacterial immunotherapeutics: Lessons from the pathogenic Neisseriae.Immunobiology · 2016Review
- A Novel Factor H-Fc Chimeric Immunotherapeutic Molecule against Neisseria gonorrhoeae.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- Defining the Binding Region in Factor H to Develop a Therapeutic Factor H-Fc Fusion Protein against Non-Typeable Haemophilus influenzae.Frontiers in cellular and infection microbiology · 2016Article
- Evolutionary insights into host-pathogen interactions from mammalian sequence data.Nature reviews. Genetics · 2015Review
- Fusion protein comprising factor H domains 6 and 7 and human IgG1 Fc as an antibacterial immunotherapeutic.Clinical and vaccine immunology : CVI · 2014Article
- Ubiquitous sialometabolism present among oral fusobacteria.PloS one · 2014Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Human factor H (HufH), a key inhibitor of the alternative pathway of complement, binds to Neisseria gonorrhoeae and constitutes an important mechanism of human-specific complement evasion. The C-terminal domain 20 of HufH contains the binding site for sialylated gonococci. We exploited differences in amino acid sequences between human and non-binding chimpanzee fH domain 20 to create cross-species mutations to define amino acids important for binding to sialylated gonococci. We used fH/Fc fusion constructs that contained contiguous fH domains 18-20 fused to Fc fragments of murine IgG2a. The Fc region was used both as a tag for detection of each fusion molecule on the bacterial surface and as an indicator for complement-dependent killing. Arg-1203 was critical for binding to both porin (Por) B.1A and PorB.1B strains. Modeling of the R1203N human-to-chimpanzee mutation using the crystal structure of HufH19-20 as a template showed a loss of positive charge that protrudes at the C terminus of domain 20. We tested the functional importance of Arg-1203 by incubating sialylated gonococci with normal human serum, in the presence of wild-type HufH18-20/Fc or its R1203A mutant. Gonococci bound and were killed by wild-type HufH18-20/Fc but not by the R1203A mutant. A recombinant fH/Fc molecule that contained chimpanzee domain 20, humanized only at amino acid 1203 (N1203R) also bound to sialylated gonococci and restored killing. These findings provide further insights into the species specificity of gonococcal infections and proof-of-concept of a novel therapeutic approach against gonorrhea, a disease rapidly becoming resistant to conventional antibiotics.
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