Increased immunogenicity and protective efficacy of influenza M2e fused to a tetramerizing protein.

The ectodomain of the matrix 2 protein (M2e) of influenza A virus represents an attractive target for developing a universal influenza A vaccine, with its sequence being highly conserved amongst human variants of this virus. With the aim of targeting conformational epitopes presumably shared by dive...

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Autores principales:	Anne-Marie Carola Andersson, Kjell O Håkansson, Benjamin Anderschou Holbech Jensen, Dennis Christensen, Peter Andersen, Allan Randrup Thomsen, Jan Pravsgaard Christensen
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9fcc58fe31204fd5913bf95deb263eb9
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spelling	oai:doaj.org-article:9fcc58fe31204fd5913bf95deb263eb92021-11-18T08:13:33ZIncreased immunogenicity and protective efficacy of influenza M2e fused to a tetramerizing protein.1932-620310.1371/journal.pone.0046395https://doaj.org/article/9fcc58fe31204fd5913bf95deb263eb92012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23049700/?tool=EBIhttps://doaj.org/toc/1932-6203The ectodomain of the matrix 2 protein (M2e) of influenza A virus represents an attractive target for developing a universal influenza A vaccine, with its sequence being highly conserved amongst human variants of this virus. With the aim of targeting conformational epitopes presumably shared by diverse influenza A viruses, a vaccine (M2e-NSP4) was constructed linking M2e (in its consensus sequence) to the rotavirus fragment NSP4(98-135); due to its coiled-coil region this fragment is known to form tetramers in aqueous solution and in this manner we hoped to mimick the natural configuration of M2e as presented in membranes. M2e-NSP4 was then evaluated side-by-side with synthetic M2e peptide for its immunogenicity and protective efficacy in a murine influenza challenge model. Here we demonstrate that M2e fused to the tetramerizing protein induces an accelerated, augmented and more broadly reactive antibody response than does M2e peptide as measured in two different assays. Most importantly, vaccination with M2e-NSP4 caused a significant decrease in lung virus load early after challenge with influenza A virus and maintained its efficacy against a lethal challenge even at very low vaccine doses. Based on the results presented in this study M2e-NSP4 merits further investigation as a candidate for or as a component of a universal influenza A vaccine.Anne-Marie Carola AnderssonKjell O HåkanssonBenjamin Anderschou Holbech JensenDennis ChristensenPeter AndersenAllan Randrup ThomsenJan Pravsgaard ChristensenPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 10, p e46395 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Anne-Marie Carola Andersson Kjell O Håkansson Benjamin Anderschou Holbech Jensen Dennis Christensen Peter Andersen Allan Randrup Thomsen Jan Pravsgaard Christensen Increased immunogenicity and protective efficacy of influenza M2e fused to a tetramerizing protein.
description	The ectodomain of the matrix 2 protein (M2e) of influenza A virus represents an attractive target for developing a universal influenza A vaccine, with its sequence being highly conserved amongst human variants of this virus. With the aim of targeting conformational epitopes presumably shared by diverse influenza A viruses, a vaccine (M2e-NSP4) was constructed linking M2e (in its consensus sequence) to the rotavirus fragment NSP4(98-135); due to its coiled-coil region this fragment is known to form tetramers in aqueous solution and in this manner we hoped to mimick the natural configuration of M2e as presented in membranes. M2e-NSP4 was then evaluated side-by-side with synthetic M2e peptide for its immunogenicity and protective efficacy in a murine influenza challenge model. Here we demonstrate that M2e fused to the tetramerizing protein induces an accelerated, augmented and more broadly reactive antibody response than does M2e peptide as measured in two different assays. Most importantly, vaccination with M2e-NSP4 caused a significant decrease in lung virus load early after challenge with influenza A virus and maintained its efficacy against a lethal challenge even at very low vaccine doses. Based on the results presented in this study M2e-NSP4 merits further investigation as a candidate for or as a component of a universal influenza A vaccine.
format	article
author	Anne-Marie Carola Andersson Kjell O Håkansson Benjamin Anderschou Holbech Jensen Dennis Christensen Peter Andersen Allan Randrup Thomsen Jan Pravsgaard Christensen
author_facet	Anne-Marie Carola Andersson Kjell O Håkansson Benjamin Anderschou Holbech Jensen Dennis Christensen Peter Andersen Allan Randrup Thomsen Jan Pravsgaard Christensen
author_sort	Anne-Marie Carola Andersson
title	Increased immunogenicity and protective efficacy of influenza M2e fused to a tetramerizing protein.
title_short	Increased immunogenicity and protective efficacy of influenza M2e fused to a tetramerizing protein.
title_full	Increased immunogenicity and protective efficacy of influenza M2e fused to a tetramerizing protein.
title_fullStr	Increased immunogenicity and protective efficacy of influenza M2e fused to a tetramerizing protein.
title_full_unstemmed	Increased immunogenicity and protective efficacy of influenza M2e fused to a tetramerizing protein.
title_sort	increased immunogenicity and protective efficacy of influenza m2e fused to a tetramerizing protein.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/9fcc58fe31204fd5913bf95deb263eb9
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Increased immunogenicity and protective efficacy of influenza M2e fused to a tetramerizing protein.

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