Giuseppe
Emeritus
[Source: PLoS ONE, full text: (LINK). Abstract, edited.]
--------
Robust Immunity and Heterologous Protection against Influenza in Mice Elicited by a Novel Recombinant NP-M2e Fusion Protein Expressed in E. coli
Wenling Wang 1, Baoying Huang 2, Tao Jiang 3, Xiuping Wang 4, Xiangrong Qi 5, Yingying Gao 6, Wenjie Tan 7, Li Ruan 8
1-8 National Institute for Viral Disease Control & Prevention, Chinese Center for Disease Control and Prevention, China CDC, Beijing, People?s Republic of China
Contributed equally to this work with: Wenling Wang, Baoying Huang
Abstract
Background
The 23-amino acid extracellular domain of matrix 2 protein (M2e) and the internal nucleoprotein (NP) of influenza are highly conserved among viruses and thus are promising candidate antigens for the development of a universal influenza vaccine. Various M2e- or NP-based DNA or viral vector vaccines have been shown to have high immunogenicity; however, high cost, complicated immunization procedures, and vector-specific antibody responses have restricted their applications. Immunization with an NP?M2e fusion protein expressed in Escherichia coli may represent an alternative strategy for the development of a universal influenza vaccine.
Methodology/Principal Findings
cDNA encoding M2e was fused to the 3′ end of NP cDNA from influenza virus A/Beijing/30/95 (H3N2). The fusion protein (NM2e) was expressed in E. coli and isolated with 90% purity. Mice were immunized with recombinant NM2e protein along with aluminum hydroxide gel and/or CpG as adjuvant. NM2e plus aluminum hydroxide gel almost completely protected the mice against a lethal (20 LD<SUB>50</SUB>) challenge of heterologous influenza virus A/PR/8/34.
Conclusions/Significance
The NM2e fusion protein expressed in E. coli was highly immunogenic in mice. Immunization with NM2e formulated with aluminum hydroxide gel protected mice against a lethal dose of a heterologous influenza virus. Vaccination with recombinant NM2e fusion protein is a promising strategy for the development of a universal influenza vaccine.
Citation: Wang W, Huang B, Jiang T, Wang X, Qi X, et al. (2012) Robust Immunity and Heterologous Protection against Influenza in Mice Elicited by a Novel Recombinant NP-M2e Fusion Protein Expressed in E. coli. PLoS ONE 7(12): e52488. doi:10.1371/journal.pone.0052488
Editor: Gourapura J. Renukaradhya, The Ohio State University, United States of America
Received: August 14, 2012; Accepted: November 13, 2012; Published: December 21, 2012
Copyright: ? 2012 Wang et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Funding: This work was supported by a grant from the National High Technology Research and Development Program of China (863 Program) (grant number 2006AA02A203). The funders had no role in study design, data collection and analysis, decision to publish, or preperation of the manuscript.
Competing interests: The authors have declared that no competing interests exist.
* E-mail: ruanl@bbn.cn
# These authors contributed equally to this work.
-Wenling Wang 1, Baoying Huang 2, Tao Jiang 3, Xiuping Wang 4, Xiangrong Qi 5, Yingying Gao 6, Wenjie Tan 7, Li Ruan 8
1-8 National Institute for Viral Disease Control & Prevention, Chinese Center for Disease Control and Prevention, China CDC, Beijing, People?s Republic of China
Contributed equally to this work with: Wenling Wang, Baoying Huang
Abstract
Background
The 23-amino acid extracellular domain of matrix 2 protein (M2e) and the internal nucleoprotein (NP) of influenza are highly conserved among viruses and thus are promising candidate antigens for the development of a universal influenza vaccine. Various M2e- or NP-based DNA or viral vector vaccines have been shown to have high immunogenicity; however, high cost, complicated immunization procedures, and vector-specific antibody responses have restricted their applications. Immunization with an NP?M2e fusion protein expressed in Escherichia coli may represent an alternative strategy for the development of a universal influenza vaccine.
Methodology/Principal Findings
cDNA encoding M2e was fused to the 3′ end of NP cDNA from influenza virus A/Beijing/30/95 (H3N2). The fusion protein (NM2e) was expressed in E. coli and isolated with 90% purity. Mice were immunized with recombinant NM2e protein along with aluminum hydroxide gel and/or CpG as adjuvant. NM2e plus aluminum hydroxide gel almost completely protected the mice against a lethal (20 LD<SUB>50</SUB>) challenge of heterologous influenza virus A/PR/8/34.
Conclusions/Significance
The NM2e fusion protein expressed in E. coli was highly immunogenic in mice. Immunization with NM2e formulated with aluminum hydroxide gel protected mice against a lethal dose of a heterologous influenza virus. Vaccination with recombinant NM2e fusion protein is a promising strategy for the development of a universal influenza vaccine.
Citation: Wang W, Huang B, Jiang T, Wang X, Qi X, et al. (2012) Robust Immunity and Heterologous Protection against Influenza in Mice Elicited by a Novel Recombinant NP-M2e Fusion Protein Expressed in E. coli. PLoS ONE 7(12): e52488. doi:10.1371/journal.pone.0052488
Editor: Gourapura J. Renukaradhya, The Ohio State University, United States of America
Received: August 14, 2012; Accepted: November 13, 2012; Published: December 21, 2012
Copyright: ? 2012 Wang et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Funding: This work was supported by a grant from the National High Technology Research and Development Program of China (863 Program) (grant number 2006AA02A203). The funders had no role in study design, data collection and analysis, decision to publish, or preperation of the manuscript.
Competing interests: The authors have declared that no competing interests exist.
* E-mail: ruanl@bbn.cn
# These authors contributed equally to this work.
--------