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Structural studies on P6 protein suggest it may not be a good vaccine candidate against Nontypable Haemophilus Influenzae
Author(s) -
Snyder Joy,
Kalmeta Breanna,
Sharma Sharad,
Pichichero Michael,
Michel Lea Vacca
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.928.10
Subject(s) - haemophilus influenzae , bacterial outer membrane , monoclonal antibody , biology , flow cytometry , microbiology and biotechnology , antibody , computational biology , immunology , escherichia coli , gene , genetics , antibiotics
Nontypable Haemophilus influenzae (NTHi) is the cause of several serious diseases, including pneumonia and otitis media; thus, the development of a vaccine against NTHi would be highly beneficial. The outer membrane protein P6 is currently a top vaccine candidate for NTHi. Past studies have demonstrated that P6 can interact with molecules both inside AND outside of the cell, but its structure suggests that it does not cross the outer cellular membrane. This apparent contradiction points to the urgent need for further studies on P6 in order to better understand its structure and membrane orientation. The overall goal of this project was to determine if P6 is surface exposed and able to interact with extracellular antibodies. To accomplish our goal, we utilized recombinant DNA technologies, ELISA experiments and flow cytometry to examine wild‐type NTHi, a P6 knock‐out and a P6 single‐mutant. The results of our preliminary experiments suggest that P6 monoclonal antibodies may be promiscuously binding to proteins other than P6. Further studies on P6's orientation in NTHi are imperative for future vaccine development. This study was funded by NIH NIDCD RO1 08671 and the Rochester Institute of Technology.