Abstract：
:H5N1 highly pathogenic avian influenza virus (HPAIV) poses a huge threat to public health and the global economy. These viruses cause systemic infection in poultry and accidental human infection leads to severe pneumonia, associated with high mortality rates. The hemagglutinin (HA) of H5N1 HPAIV possesses multiple basic amino acids, as in the sequence RERRRKKR at the cleavage site; however, the role of this motif is not fully understood. Here, we showed that a 33-amino acid long peptide derived from HA of H5N1 HPAIV (HA314-46) has the potential to penetrate various cells and lung tissue through a sialic acid-independent endocytotic pathway. Mutant peptide analyses revealed that the cysteine residue at position 318 and multiple basic amino acids were essential for the cell-penetrating activity. Moreover, reassortant viruses possessing H5 HA could enter sialic acid-deficient cells, and virus internalisation was facilitated by cleavage with recombinant furin. Thus, our findings demonstrate that the HA314-46 motif exhibits cell-penetrating activity through a sialic acid-independent cell entry mechanism.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Kajiwara N,Nomura N,Ukaji M,Yamamoto N,Kohara M,Yasui F,Sakoda Y,Kida H,Shibasaki Fdoi
10.1038/s41598-020-74604-wsubject
Has Abstractpub_date
2020-10-22 00:00:00pages
18008issue
1issn
2045-2322pii
10.1038/s41598-020-74604-wjournal_volume
10pub_type
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