Evidence that Receptor Destruction by the Sendai Virus Hemagglutinin-Neuraminidase Protein Is Responsible for Homologous Interference.
Receptor destruction has been considered one of the mechanisms of homologous Sendai virus (SeV) interference. However, direct evidence of receptor destruction upon virus infection and its relevance to interference is missing. To investigate a precise mechanism of homologous interference, we established SeV persistently infected cells. The persistently infected cells inhibited superinfection by homologous SeV but supported replication of human parainfluenza virus 2 (hPIV2) and influenza A virus (IAV). We confirmed that SeV particles could not attach to or penetrate the infected cells and that the hemagglutinin-neuraminidase (HN) protein of SeV was involved in the interference. Lectin blot assays showed that the α2,3-linked sialic acids were specifically reduced in the SeV-infected cells, but the level of α2,6-linked sialic acids had not changed. As infection with IAV removed both α2,3- and α2,6-linked sialic acids, especially α2,3-linked sialic acids, IAV-infected cells inhibited superinfection of SeV. These results provide concrete evidence that destruction of the specific SeV receptor, α2,3-linked sialic acids, is relevant to homologous interference by SeV.



Viral interference is a classically observed phenomenon, but the precise mechanism is not clear. Using SeV interference, we provide concrete evidence that reduction of the α2,3-linked sialic acid receptor by the HN of SeV is closely related with viral interference. Since SeV infection resulted in decrease of only α2,3-linked sialic acids, IAV, which also utilized α2,6-linked sialic acids to initiate infection, superinfected the SeV-infected cells. In contrast, SeV could not superinfect the IAV-infected cells because both α2,3- and α2,6-linked sialic acids were removed. These results indicate that receptor destruction critically contributes to viral interference.
Department of Microbiology, School of Medicine, Wakayama Medical University, Wakayama, Japan.
Hideo
H
Goto
Department of Microbiology, School of Medicine, Wakayama Medical University, Wakayama, Japan.
Keisuke
K
Ohta
Department of Microbiology, School of Medicine, Wakayama Medical University, Wakayama, Japan.
Yusuke
Y
Matsumoto
Department of Microbiology, School of Medicine, Wakayama Medical University, Wakayama, Japan.
Natsuko
N
Yumine
Department of Microbiology, School of Medicine, Wakayama Medical University, Wakayama, Japan mnishio@wakayama-med.ac.jp.
Machiko
M
Nishio
D000818:Animals; D002460:Cell Line; D015707:HN Protein / Q000378:metabolism*; D006801:Humans; D009980:Influenza A virus / Q000254:growth & development; D010223:Parainfluenza Virus 2, Human / Q000254:growth & development; D011991:Receptors, Virus / Q000378:metabolism*; D029082:Sendai virus / Q000201:enzymology* / Q000502:physiology*; D012794:Sialic Acids / Q000378:metabolism; D014762:Viral Interference
D015707:HN Protein; C039111:HN protein receptor; D011991:Receptors, Virus; D012794:Sialic Acids