scholarly journals Outer Membrane Proteins as a Carrier for Detoxified Lipooligosaccharide Conjugate Vaccines for NontypeableHaemophilus influenzae

1999 ◽  
Vol 67 (10) ◽  
pp. 5508-5513 ◽  
Author(s):  
Ting-Huai Wu ◽  
Xin-Xing Gu
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Respiratory Tract Infections ◽  
Outer Membrane Proteins ◽  
Surface Antigens ◽  
Conjugate Vaccines ◽  
Vaccine Candidates ◽  
Potential Vaccine ◽  
Major Surface ◽  
Tract Infections

ABSTRACT Nontypeable Haemophilus influenzae (NTHi) is a common cause of otitis media and respiratory tract infections. Outer membrane proteins (OMP) and lipooligosaccharide (LOS) are major surface antigens of NTHi and potential vaccine candidates. De-O-acylated LOS (dLOS) or oligosaccharide (OS) was coupled to total OMP to form dLOS-OMP and OS-OMP conjugates, while a dLOS-tetanus toxoid (TT) was synthesized for comparison. These conjugates were evaluated in mice and rabbits for immunogenicity. dLOS-OMP elicited a better boostable antibody response against LOS than did dLOS-TT, while OS-OMP was not immunogenic. Formulation of the conjugates with Ribi adjuvant significantly enhanced the immunogenicity of dLOS-OMP and dLOS-TT but not that of OS-OMP. In addition, rabbit antisera elicited by dLOS-OMP but not dLOS-TT (or OMP alone) demonstrated bactericidal activity against 40% of the NTHi strains tested. These results indicate that dLOS is a better derivative of LOS than OS and that OMP is a good carrier for NTHi LOS-based conjugate vaccines.

Immunogenicity of the recombinant leptospiral putative outer membrane proteins as vaccine candidates

Vaccine ◽  
2007 ◽  
Vol 25 (48) ◽  
pp. 8190-8197 ◽  
Author(s):  
Yung-Fu Chang ◽  
Chia-Sui Chen ◽  
Raghavan U.M. Palaniappan ◽  
Hongxuan He ◽  
Sean P. McDonough ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Vaccine Candidates

Immunoproteomic Identification of Polyvalent Vaccine Candidates from Vibrio parahaemolyticus Outer Membrane Proteins

2010 ◽  
Vol 9 (5) ◽  
pp. 2573-2583 ◽  
Author(s):  
Hui Li ◽  
Ming-Zhi Ye ◽  
Bo Peng ◽  
Hong-Kai Wu ◽  
Chang-Xin Xu ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Vibrio Parahaemolyticus ◽  
Outer Membrane Proteins ◽  
Vaccine Candidates ◽  
Polyvalent Vaccine

scholarly journals Physical Linkage of Naturally Complexed Bacterial Outer Membrane Proteins Enhances Immunogenicity

2007 ◽  
Vol 76 (3) ◽  
pp. 1223-1229 ◽  
Author(s):  
Henriette Macmillan ◽  
Junzo Norimine ◽  
Kelly A. Brayton ◽  
Guy H. Palmer ◽  
Wendy C. Brown
Keyword(s):  
T Cell ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Surface Protein ◽  
Host Cells ◽  
Effective Vaccine ◽  
T Cell Epitopes ◽  
Carrier Effect ◽  
Major Surface

ABSTRACTThe outer membrane proteins (OMPs) of bacterial pathogens are essential for their growth and survival and especially for attachment and invasion of host cells. Since the outer membrane is the interface between the bacterium and the host cell, outer membranes and individual OMPs are targeted for development of vaccines against many bacterial diseases. Whole outer membrane fractions often protect against disease, and this protection cannot be fully reproduced by using individual OMPs. Exactly how the interactions among individual OMPs influence immunity is not well understood. We hypothesized that one OMP rich in T-cell epitopes can act as a carrier for an associated OMP which is poor in T-cell epitopes to generate T-dependent antibody responses, similar to the hapten-carrier effect. Major surface protein 1a (MSP1a) and MSP1b1 occur as naturally complexed OMPs in theAnaplasma marginaleouter membrane. Previous studies demonstrated that immunization with the native MSP1 heteromer induced strong immunoglobulin G (IgG) responses to both proteins, but only MSP1a stimulated strong CD4+T-cell responses. Therefore, to test our hypothesis, constructs of CD4+T-cell epitopes from MSP1a linked to MSP1b1 were compared with individually administered MSP1a and MSP1b1 for induction of MSP1b-specific IgG. By linking the T-cell epitopes from MSP1a to MSP1b1, significantly higher IgG titers against MSP1b1 were induced. Understanding how the naturally occurring intermolecular interactions between OMPs influence the immune response may lead to more effective vaccine design.

Sign in / Sign up

Export Citation Format

Share Document