Abstract：
:The membrane fusion potential of influenza HA, like many viral membrane-fusion glycoproteins, is generated by proteolytic cleavage of a biosynthetic precursor. The three-dimensional structure of ectodomain of the precursor HA0 has been determined and compared with that of cleaved HA. The cleavage site is a prominent surface loop adjacent to a novel cavity; cleavage results in structural rearrangements in which the nonpolar amino acids near the new amino terminus bury ionizable residues in the cavity that are implicated in the low-pH-induced conformational change. Amino acid insertions at the cleavage site in HAs of virulent avian viruses and those of viruses isolated from the recent severe outbreak of influenza in humans in Hong Kong would extend this surface loop, facilitating intracellular cleavage.
journal_name
Celljournal_title
Cellauthors
Chen J,Lee KH,Steinhauer DA,Stevens DJ,Skehel JJ,Wiley DCdoi
10.1016/s0092-8674(00)81771-7subject
Has Abstractpub_date
1998-10-30 00:00:00pages
409-17issue
3eissn
0092-8674issn
1097-4172pii
S0092-8674(00)81771-7journal_volume
95pub_type
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