pH-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin

We previously reported the expression of soluble A/Victoria/3/75 (H3N2) hemagglutinin in insect cells and the molecular and immunological structure of an aggregated fraction, only observed in cell supernatant when expression was performed at low pH [23]. Here we report that besides this aggregated a...

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Autores principales: Vanlandschoot, P., Beirnaert, E., Grooten, J., Min Jou, W., Fiers, W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer-Verlag 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7086992/
https://www.ncbi.nlm.nih.gov/pubmed/9541609
http://dx.doi.org/10.1007/s007050050282
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author Vanlandschoot, P.
Beirnaert, E.
Grooten, J.
Min Jou, W.
Fiers, W.
author_facet Vanlandschoot, P.
Beirnaert, E.
Grooten, J.
Min Jou, W.
Fiers, W.
author_sort Vanlandschoot, P.
collection PubMed
description We previously reported the expression of soluble A/Victoria/3/75 (H3N2) hemagglutinin in insect cells and the molecular and immunological structure of an aggregated fraction, only observed in cell supernatant when expression was performed at low pH [23]. Here we report that besides this aggregated a monomeric and possibly a trimeric structure is detected in cell supernatant, irrespective of the pH of the medium. Evidence is presented that the aggregated fraction is generated out of monomeric HA0s molecules due to a low intracellular pH encountered during secretion.
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spelling pubmed-70869922020-03-23 pH-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin Vanlandschoot, P. Beirnaert, E. Grooten, J. Min Jou, W. Fiers, W. Arch Virol Article We previously reported the expression of soluble A/Victoria/3/75 (H3N2) hemagglutinin in insect cells and the molecular and immunological structure of an aggregated fraction, only observed in cell supernatant when expression was performed at low pH [23]. Here we report that besides this aggregated a monomeric and possibly a trimeric structure is detected in cell supernatant, irrespective of the pH of the medium. Evidence is presented that the aggregated fraction is generated out of monomeric HA0s molecules due to a low intracellular pH encountered during secretion. Springer-Verlag 2014-04-07 1998 /pmc/articles/PMC7086992/ /pubmed/9541609 http://dx.doi.org/10.1007/s007050050282 Text en © Springer-Verlag 1998 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Article
Vanlandschoot, P.
Beirnaert, E.
Grooten, J.
Min Jou, W.
Fiers, W.
pH-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin
title pH-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin
title_full pH-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin
title_fullStr pH-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin
title_full_unstemmed pH-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin
title_short pH-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin
title_sort ph-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7086992/
https://www.ncbi.nlm.nih.gov/pubmed/9541609
http://dx.doi.org/10.1007/s007050050282
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AT minjouw phdependentaggregationandsecretionofsolublemonomericinfluenzahemagglutinin
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