Hemagglutinin structure, membrane fusion and virus entry

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F15%3A43907751" target="_blank" >RIV/62156489:43210/15:43907751 - isvavai.cz</a>

Result on the web

<a href="http://web2.mendelu.cz/af_239_nanotech/J_Met_Nano/0115/pdf/JMN1-2015-9.pdf" target="_blank" >http://web2.mendelu.cz/af_239_nanotech/J_Met_Nano/0115/pdf/JMN1-2015-9.pdf</a>

DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Hemagglutinin structure, membrane fusion and virus entry

Original language description

Hemagglutinin (HA) is an antigenic glycoprotein, which is placed on the surface of the influenza viruses. It is responsible for binding the virus to the host cell, that is being infected. The name ""hemagglutinin"" comes from the ability of protein to cause erythrocytes to agglutinate (""clump together""). The process is like this: Hemagglutinin (HA) binds to the monosaccharide sialic acid which is present on the surface of its target host cells. The cell membrane then engulfs the virus through endocytosis and followed by formation of endosome. The cell then attempts to begin digesting the contents of the endosome by acidifying its interior and transforming it into a lysosome. When the pH decrease to 6.0, the HA molecule becomes partially unfold, and release a hydrophobic portion of peptide chain that was previously hidden. This so-called ""fusion peptide"" acts like a molecular grapple hook for lock on the endosomal membrane. The rest of the HA molecule refolds into a new structure an

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EE - Microbiology, virology

OECD FORD branch

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Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2015

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Metallomics and Nanotechnologies

ISSN

2336-3940

e-ISSN

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Volume of the periodical

2

Issue of the periodical within the volume

1

Country of publishing house

CZ - CZECH REPUBLIC

Number of pages

4

Pages from-to

53-56

UT code for WoS article

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EID of the result in the Scopus database

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