• Han-Qing Jiang, Susan K Hoiseth, Shannon L Harris, Lisa K McNeil, Duzhang Zhu, Cuiwen Tan, Adrienne A Scott, Kristin Alexander, Kathryn Mason, Lynn Miller, Ida DaSilva, Michelle Mack, Xiao-Juan Zhao, Michael W Pride, Lubomira Andrew, Ellen Murphy, Michael Hagen, Roger French, Ashoni Arora, Thomas R Jones, Kathrin U Jansen, Gary W Zlotnick, and Annaliesa S Anderson.
• Pfizer Vaccine Research, 401N. Middletown Rd., Pearl River, NY 10965, USA.
• Vaccine. 2010 Aug 23; 28 (37): 6086-93.

AbstractFactor H binding proteins (fHBP), are bacterial surface proteins currently undergoing human clinical trials as candidate serogroup B Neisseria meningitidis (MnB) vaccines. fHBP protein sequences segregate into two distinct subfamilies, designated A and B. Here, we report the specificity and vaccine potential of mono- or bivalent fHBP-containing vaccines. A bivalent fHBP vaccine composed of a member of each subfamily elicited substantially broader bactericidal activity against MnB strains expressing heterologous fHBP than did either of the monovalent vaccines. Bivalent rabbit immune sera tested in serum bactericidal antibody assays (SBAs) against a diverse panel of MnB clinical isolates killed 87 of the 100 isolates. Bivalent human immune sera killed 36 of 45 MnB isolates tested in SBAs. Factors such as fHBP protein variant, PorA subtype, or MLST were not predictive of whether the MnB strain could be killed by rabbit or human immune sera. Instead, the best predictor for killing in the SBA was the level of in vitro surface expression of fHBP. The bivalent fHBP vaccine candidate induced immune sera that killed MnB isolates representing the major MLST complexes, prevalent PorA subtypes, and fHBP variants that span the breadth of the fHBP phylogenetic tree. Importantly, epidemiologically prevalent fHBP variants from both subfamilies were killed.Copyright 2010 Elsevier Ltd. All rights reserved.

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