Structural, functional and immunogenic insights on Cu,Zn superoxide dismutase pathogenic virulence factors from Neisseria meningitidis and Brucella abortus

Pratt, Ashley J.; DiDonato, Michael; Shin, David S.; Cabelli, Diane E.; Bruns, Cami K.; Belzer, Carol A.; Gorringe, Andrew R.; Langford, Paul R.; Tabatabai, Louisa B.; Kroll, J. Simon; Tainer, John A.; Getzoff, Elizabeth D.

doi:10.1128/JB.00343-15

Title: Structural, functional and immunogenic insights on Cu,Zn superoxide dismutase pathogenic virulence factors from Neisseria meningitidis and Brucella abortus

Journal Article · Mon Oct 12 00:00:00 EDT 2015 · Journal of Bacteriology

DOI:https://doi.org/10.1128/JB.00343-15· OSTI ID:1224775

Pratt, Ashley J. ^[1]; DiDonato, Michael ^[2]; Shin, David S. ^[1]; Cabelli, Diane E. ^[3]; Bruns, Cami K. ^[2]; Belzer, Carol A. ^[4]; Gorringe, Andrew R. ^[5]; Langford, Paul R. ^[6]; Tabatabai, Louisa B. ^[4]; Kroll, J. Simon ^[6]; Tainer, John A. ^[7]; Getzoff, Elizabeth D. ^[2]

The Scripps Research Institute, La Jolla, CA (United States); Lawrence Berkeley National Lab., Berkeley, CA (United States)
The Scripps Research Institute, La Jolla, CA (United States)
Brookhaven National Lab. (BNL), Upton, NY (United States)
National Animal Disease Center, Ames, IA (United States)
Public Health England (previously The Health Protection Agency), Salisbury (United Kingdom)
Imperial College, London (United Kingdom)
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Univ. of Texas M.D. Anderson Cancer Center, Houston, TX (United States)

Bacterial pathogens Neisseria meningitidis and Brucella abortus pose threats to human and animal health worldwide, causing meningococcal disease and brucellosis, respectively. Mortality from acute N. meningitidis infections remains high despite antibiotics, and brucellosis presents alimentary and health consequences. Superoxide dismutases are master regulators of reactive oxygen and general pathogenicity factors and are therefore therapeutic targets. Cu,Zn superoxide dismutases (SODs) localized to the periplasm promote survival by detoxifying superoxide radicals generated by major host antimicrobial immune responses. We discovered that passive immunization with an antibody directed at N. meningitidis SOD (NmSOD) was protective in a mouse infection model. To define the relevant atomic details and solution assembly states of this important virulence factor, we report high-resolution and X-ray scattering analyses of NmSOD and of SOD from B. abortus (BaSOD). The NmSOD structures revealed an auxiliary tetrahedral Cu-binding site bridging the dimer interface; mutational analyses suggested that this metal site contributes to protein stability, with implications for bacterial defense mechanisms. Biochemical and structural analyses informed us about electrostatic substrate guidance, dimer assembly, and an exposed C-terminal epitope in the NmSOD dimer. In contrast, the monomeric BaSOD structure provided insights for extending immunogenic peptide epitopes derived from the protein. These collective results reveal unique contributions of SOD to pathogenic virulence, refine predictive motifs for distinguishing SOD classes, and suggest general targets for antibacterial immune responses. Furthermore, the identified functional contributions, motifs, and targets distinguishing bacterial and eukaryotic SOD assemblies presented here provide a foundation for efforts to develop SOD-specific inhibitors of or vaccines against these harmful pathogens.

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Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: SC0012704

OSTI ID:: 1224775

Alternate ID(s):: OSTI ID: 1235891

Report Number(s):: BNL-108508-2015-JA; BNL-111744-2016-JA; R&D Project: CO004; KC0304030

Journal Information:: Journal of Bacteriology, Vol. 197, Issue 24; ISSN 0021-9193

Publisher:: American Society for MicrobiologyCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 14 works

Citation information provided by
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