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Recombinant truncated E protein as a new vaccine candidate against nontypeable H. influenzae: Its expression and immunogenic evaluation.

Abstract：

:Protein E (PE) is a conserved entity observed in both nontypeable Haemophilus influenzae (NTHi) and encapsulated H. influenzae. This is a small surface lipoprotein, consisting of only 160 amino acids, involved in the adhesion of H. influenzae to various types of epithelial cells. A 384-bp-long fragment from NTHi PE was cloned into the prokaryotic expression vector pBAD-gIIIA. The recombinant protein was expressed with arabinose and then purified by affinity purification on an Ni-NTA agarose matrix. BALB/c mice were immunized by subcutaneous injection with purified recombinant truncated PE mixed with an alum adjuvant. Serum antibody response and the functional activity of antibodies were evaluated by enzyme-linked immunosorbent assay (ELISA) and serum bactericidal assay (SBA), respectively. Colony PCR, double digestion, and sequencing were used to verify successful cloning of truncated PE. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and western blot analyses indicated the presence of a ∼15-kDa recombinant protein. Serum IgG, IgG1, and IgG2a levels were significantly higher in the group immunized by recombinant truncated PE mixed with an alum adjuvant, compared to the non-vaccinated control group. Development of a strong bactericidal effect against NTHi was observed in the serum samples from immunized animals. Our findings suggest that recombinant truncated PE is a potential vaccine candidate for NTHi.

journal_name

Microb Pathog

journal_title

Microbial pathogenesis

authors

Behrouzi A,Bouzari S,Vaziri F,Fateh A,Afrough P,Vijeh Motlagh AD,Siadat SD

doi

10.1016/j.micpath.2017.07.025

subject

Has Abstract

pub_date

2017-09-01 00:00:00

pages

431-438

eissn

0882-4010

issn

1096-1208

pii

S0882-4010(16)30575-7

journal_volume

110

pub_type

杂志文章

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