Zusammenfassung
SER virus is a member of the family Paramyxoviridae, genus Rubulavirus,
which has been isolated from pigs. It is very closely related to
SV5 virus serologically, in protein profile, and in nucleotide sequence.
However, unlike SV5, SER induces minimal syncytium formation in infected
CV-1 or BHK cells. Fluorescence transfer experiments between labeled
erythrocytes and infected MDBK cells revealed that SER also induces
hemifusion and pore formation with reduced efficiency. The virion
polypeptide profiles of SER and SV5 are very similar, except that
the SER F1 subunit shows an apparent molecular weight that is about
2 kDa higher than that of SV5. Comparison of the deduced amino acid
sequences revealed the SER F (551 aa) to be longer than SV5 F (529
aa) by 22 residues in the cytoplasmic tail (CT) domain. The HN and
M gene sequences of the viruses were found to be very similar. The
SER F showed minimal fusion activity when coexpressed with either
SV5 or SER HN. In contrast, SV5 F was highly fusogenic when coexpressed
with either HN protein, indicating that the restricted fusion capacity
of SER virus is a property of its F protein. Truncation in the CT
of SER F by 22 residues completely rescued its ability to cause syncytium
formation, whereas other truncations rescued syncytium formation
partially. These results demonstrate that an elongated CT of a paramyxovirus
F protein suppresses its membrane fusion activity.
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