Detail
Article
Online article
FT
Medvik - BMC
  • Something wrong with this record ?

Hemagglutinin structure, membrane fusion and virus entry

Petr Michalek, Ludmila Krejcova, Vojtech Adam, Rene Kizek

Language English Country Czech Republic

Document type Review, Research Support, Non-U.S. Gov't

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 and pulls the endosomal membrane right up next to the viral membrane, causing the two to fuse together. When it happened, the viral RNA genome enters into the cell‘s cytoplasm.

000      
00000naa a2200000 a 4500
001      
bmc16016217
003      
CZ-PrNML
005      
20160721114244.0
007      
cr|cn|
008      
160606s2015 xr fs 000 0|eng||
009      
AR
040    __
$a ABA008 $d ABA008 $e AACR2 $b cze
041    0_
$a eng
044    __
$a xr
100    1_
$a Michálek, Petr $7 _AN082249 $u Department of Chemistry and Biochemistry, Mendel University in Brno, Czech Republic, European Union
245    10
$a Hemagglutinin structure, membrane fusion and virus entry / $c Petr Michalek, Ludmila Krejcova, Vojtech Adam, Rene Kizek
520    3_
$a 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 and pulls the endosomal membrane right up next to the viral membrane, causing the two to fuse together. When it happened, the viral RNA genome enters into the cell‘s cytoplasm.
650    _2
$a lidé $7 D006801
650    12
$a hemaglutininové glykoproteiny viru chřipky $x imunologie $7 D019267
650    _2
$a hemaglutininy $x imunologie $7 D006388
650    12
$a virus chřipky A $x imunologie $x patogenita $7 D009980
650    _2
$a fúze membrán $7 D008561
650    _2
$a buněčná membrána $7 D002462
650    12
$a internalizace viru $7 D053586
655    _2
$a přehledy $7 D016454
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Krejčová, Ludmila $7 _AN074759 $u Department of Chemistry and Biochemistry, Mendel University in Brno, Czech Republic, European Union
700    1_
$a Adam, Vojtěch, $d 1982- $7 xx0064599 $u Department of Chemistry and Biochemistry, Mendel University in Brno, Czech Republic, European Union; Central European Institute of Technology, Brno University of Technology, Czech Republic, European Union
700    1_
$a Kizek, René, $d 1972- $7 jn20001005291 $u Department of Chemistry and Biochemistry, Mendel University in Brno, Czech Republic, European Union; Central European Institute of Technology, Brno University of Technology, Czech Republic, European Union
773    0_
$t Journal of Metallomics and Nanotechnologies $x 2336-3940 $g Roč. 2, č. 1 (2015), s. 53-56 $w MED00185603
856    41
$u http://web2.mendelu.cz/af_239_nanotech/J_Met_Nano/0115/pdf/JMN1-2015-9.pdf $y plný text volně přístupný
910    __
$a ABA008 $b online $c 398 $y 4 $z 0
990    __
$a 20160606103820 $b ABA008
991    __
$a 20160721114456 $b ABA008
999    __
$a ok $b bmc $g 1126810 $s 940675
BAS    __
$a 3 $a 4
BMC    __
$a 2015 $b 2 $c 1 $d 53-56 $i 2336-3940 $m Journal of Metallomics and Nanotechnologies $x MED00185603
LZP    __
$c NLK188 $d 20160721 $a NLK 2016-22/pk

Find record

Citation metrics

Loading data ...

Archiving options

Loading data ...