Influenza A hemagglutinin C-terminal anchoring peptide: identification and mass spectrometric study.
MALDI-TOF MS and N-terminal amino acid sequencing allowed us to identify several fragments of the C-terminal peptide of Influenza A hemagglutinin (HA) containing transmembrane domains (TMD). These fragments were detected in the organic phase of chloroform-methanol extracts from bromelain-treated virus particles. Heterogeneous fatty acylation of the C-terminus was revealed. Tritium bombardment technique might open an opportunity for 3D structural investigation of the HA TMD in situ.
Kordyukova
Larisa V
LV
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia. kord@belozersky.msu.ru
Ksenofontov
Aleksander L
AL
Serebryakova
Marina V
MV
Ovchinnikova
Tatyana V
TV
Fedorova
Natalija V
NV
Ivanova
Valeria T
VT
Baratova
Ludmila A
LA
D000595:Amino Acid Sequence; D000818:Animals; D001963:Bromelains; D002642:Chick Embryo; D002725:Chloroform; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D009980:Influenza A virus / Q000737:chemistry*; D000432:Methanol; D008969:Molecular Sequence Data; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D002725:Chloroform; D001963:Bromelains; D000432:Methanol