Unknown

Dataset Information

0

In silico studies of outer membrane of Neisseria meningitidis por a: its expression and immunogenic properties.


ABSTRACT: Neisseria meningitidis is a major causative agent of bacterial septicemia and meningitis in humans. Currently, there are no vaccines to prevent disease caused by strains of N.meningitidis serogroup B. The Class 1 Outer Membrane Protein (OMP) has been named porA which is a cation selective transmembrane protein of 45 KDa that forms trimeric pore in the meningococcal outer membrane. PorA from serogroup B N. meningitidis was cloned into prokaryotic expression vector pBAD-gIIIA. Recombinant protein was expressed with arabinose and affinity purified by Ni-NTA agarose, SDS-PAGE and western blotting were performed for protein determination and verification. BALB/c mice were immunized subcutaneously with purified rPorA together with alum adjuvant. Serum antibody responses to serogroups B N.meningitidis were determined by ELISA. Serum IgG response significantly increased in the group immunized with rPorA together with alum adjuvant in comparison with control groups. These results suggest that rPorA can be a potential vaccine candidate for serogroup B N.meningitidis.

SUBMITTER: Behrouzi A 

PROVIDER: S-EPMC4170490 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

altmetric image

Publications

In silico studies of outer membrane of Neisseria meningitidis por a: its expression and immunogenic properties.

Behrouzi Ava A   Bouzari Saeid S   Siadat Seyed Davar SD   Irani Shiva S  

International journal of molecular and cellular medicine 20140101 3


Neisseria meningitidis is a major causative agent of bacterial septicemia and meningitis in humans. Currently, there are no vaccines to prevent disease caused by strains of N.meningitidis serogroup B. The Class 1 Outer Membrane Protein (OMP) has been named porA which is a cation selective transmembrane protein of 45 KDa that forms trimeric pore in the meningococcal outer membrane. PorA from serogroup B N. meningitidis was cloned into prokaryotic expression vector pBAD-gIIIA. Recombinant protein  ...[more]

Similar Datasets

| S-EPMC6867985 | biostudies-literature
| S-EPMC257557 | biostudies-other
| S-EPMC3202590 | biostudies-literature
| S-EPMC2884949 | biostudies-literature
| S-EPMC3669287 | biostudies-literature
| S-EPMC6171317 | biostudies-literature
| S-EPMC2895646 | biostudies-literature