Peter Beernink, PhD
My laboratory is focused on understanding specific molecular interactions between host and pathogen, in particular between complement Factor H and Neisserial surface proteins. These investigations are directly applicable for developing improved vaccines for prevention of disease caused by the bacteria from the genus Neisseria. These microbes colonize mucous membranes, which can lead to invasive infections including sepsis, meningitis, urethritis and other infections. Our research includes genetic, biochemical and immunological studies of Neisserial surface antigens, including meningococcal Factor H binding protein and Neisserial surface protein A. These proteins are important for virulence because they recruit complement Factor H to the bacterial surface, which enables the bacteria to evade host immunity. Our studies are expected to elucidate mechanisms of pathogenesis and protective antibody function and to lead to next-generation Neisserial vaccines.
Postdoc, 03/1999 - Physical Biochemistry, University of California
Ph.D., 06/1995 - Molecular Biology and Biochemistry, Boston University
A.B., 05/1988 - Microbial Genetics, Cornell University
Honors and Awards
- Scientific Career Achievement Award, UCSF Benioff Children's Hospital Oakland, 2021
- Clorox Endowed Chair of Immunobiology and Vaccine Development, UCSF Benioff Children's Hospital Oakland, 2020
- Scientific Achievement Award, Children's Hospital & Research Center at Oakland, 2016
- Individual National Research Service Award (F32), U.C. Berkeley, 1998-2000
- Two human antibodies to a meningococcal serogroup B vaccine antigen enhance binding of complement Factor H by stabilizing the Factor H binding site.
- Broad vaccine protection against Neisseria meningitidis using factor H binding protein.
- Effect of complement Factor H on antibody repertoire and protection elicited by meningococcal capsular group B vaccines containing Factor H binding protein.
- Anti-Factor H Antibody Reactivity in Young Adults Vaccinated with a Meningococcal Serogroup B Vaccine Containing Factor H Binding Protein.
- A Meningococcal Outer Membrane Vesicle Vaccine with Overexpressed Mutant FHbp Elicits Higher Protective Antibody Responses in Infant Rhesus Macaques than a Licensed Serogroup B Vaccine.
- A Meningococcal Native Outer Membrane Vesicle Vaccine With Attenuated Endotoxin and Overexpressed Factor H Binding Protein Elicits Gonococcal Bactericidal Antibodies.
- Molecular characterization of two sub-family specific monoclonal antibodies to meningococcal Factor H binding protein.
- Crystal structure reveals vaccine elicited bactericidal human antibody targeting a conserved epitope on meningococcal fHbp.
- Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.
- Neisseria meningitidis factor H-binding protein bound to monoclonal antibody JAR5: implications for antibody synergy.
- Enhanced protective antibody to a mutant meningococcal factor H-binding protein with low-factor H binding.
- Human IgG1, IgG3, and IgG3 Hinge-Truncated Mutants Show Different Protection Capabilities against Meningococci Depending on the Target Antigen and Epitope Specificity.
- Meningococcal Factor H Binding Protein Vaccine Antigens with Increased Thermal Stability and Decreased Binding of Human Factor H.
- A meningococcal vaccine antigen engineered to increase thermal stability and stabilize protective epitopes.
- Effect of complement Factor H on anti-FHbp serum bactericidal antibody responses of infant rhesus macaques boosted with a licensed meningococcal serogroup B vaccine.
- Susceptibility of Meningococcal Strains Responsible for Two Serogroup B Outbreaks on U.S. University Campuses to Serum Bactericidal Activity Elicited by the MenB-4C Vaccine.
- A Newly-Identified Polymorphism in Rhesus Macaque Complement Factor H Modulates Binding Affinity for Meningococcal FHbp.
- Functional Analysis of the Human Antibody Response to Meningococcal Factor H Binding Protein.
- A Mutant Library Approach to Identify Improved Meningococcal Factor H Binding Protein Vaccine Antigens.
- Binding of Complement Factor H (FH) Decreases Protective Anti-FH Binding Protein Antibody Responses of Infant Rhesus Macaques Immunized With a Meningococcal Serogroup B Vaccine.
- Heterogeneity in rhesus macaque complement factor H binding to meningococcal factor H binding protein (FHbp) informs selection of primates to assess immunogenicity of FHbp-based vaccines.
- Meningococcal factor H-binding protein vaccines with decreased binding to human complement factor H have enhanced immunogenicity in human factor H transgenic mice.
- Does binding of complement factor H to the meningococcal vaccine antigen, factor H binding protein, decrease protective serum antibody responses?
- Importance of inhibition of binding of complement factor H for serum bactericidal antibody responses to meningococcal factor H-binding protein vaccines.
- Design of meningococcal factor H binding protein mutant vaccines that do not bind human complement factor H.
- The effect of human factor H on immunogenicity of meningococcal native outer membrane vesicle vaccines with over-expressed factor H binding protein.
- Monoclonal antibodies to meningococcal factor H binding protein with overlapping epitopes and discordant functional activity.
- A meningococcal factor H binding protein mutant that eliminates factor H binding enhances protective antibody responses to vaccination.
- Effect of factor H-binding protein sequence variation on factor H binding and survival of Neisseria meningitidis in human blood.
- Impaired immunogenicity of a meningococcal factor H-binding protein vaccine engineered to eliminate factor h binding.
- Frequency of factor H-binding protein modular groups and susceptibility to cross-reactive bactericidal activity in invasive meningococcal isolates.
- The modular architecture of meningococcal factor H-binding protein.
- Meningococcal factor H-binding protein variants expressed by epidemic capsular group A, W-135, and X strains from Africa.
- A region of the N-terminal domain of meningococcal factor H-binding protein that elicits bactericidal antibody across antigenic variant groups.
- Fine antigenic specificity and cooperative bactericidal activity of monoclonal antibodies directed at the meningococcal vaccine candidate factor h-binding protein.
- Bactericidal antibody responses induced by meningococcal recombinant chimeric factor H-binding protein vaccines.
- Identification of a thermo-regulated glutamine-binding protein from Yersinia pestis.
- Prevalence of factor H-binding protein variants and NadA among meningococcal group B isolates from the United States: implications for the development of a multicomponent group B vaccine.
- Applications of functional protein microarrays: identifying protein-protein interactions in an array format.
- Rapid genetic grouping of factor h-binding protein (genome-derived neisserial antigen 1870), a promising group B meningococcal vaccine candidate.
- Specificity of protein interactions mediated by BRCT domains of the XRCC1 DNA repair protein.
- High-throughput, fluorescence-based screening for soluble protein expression.
- Identification of chromatin-related protein interactions using protein microarrays.
- Thermodynamic analysis of the dissociation of the aldolase tetramer substituted at one or both of the subunit interfaces.
- Spatial clustering of isozyme-specific residues reveals unlikely determinants of isozyme specificity in fructose-1,6-bisphosphate aldolase.
- Application of In Vitro Protein Expression to Human Prote.
- Structural basis for a change in substrate specificity: crystal structure of S113E isocitrate dehydrogenase in a complex with isopropylmalate, Mg2+, and NADP.
- Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism.
- Random circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and function.
- Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation.
- Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit.
- Disruption of the aldolase A tetramer into catalytically active monomers.
- Subunit interface mutants of rabbit muscle aldolase form active dimers.
- Construction of a high-copy "ATG vector" for expression in Escherichia coli.