Sendai virus utilizes specific sialyloligosaccharides as host cell receptor determinants

Area of Science:

• Virology
• Glycobiology
• Cell Biology

Background:

• Paramyxoviruses, like Sendai virus, infect host cells by interacting with cell surface receptors.
• Sialic acids on cell surface glycans are known to play a role in viral binding and entry.
• The precise structure of sialyloligosaccharide determinants involved in Sendai virus infection remains to be fully elucidated.

Purpose of the Study:

• To investigate the role of specific sialyloligosaccharide sequences in host cell susceptibility to Sendai virus infection.
• To determine if defined sialyloligosaccharide structures act as functional receptors for Sendai virus.

Main Methods:

• Purified sialyltransferases and neuraminidase were used to enzymatically modify cell surface glycans.
• Madin-Darby bovine kidney cells were treated to remove or add specific sialic acid linkages.
• Sendai virus infection was assessed by hemagglutination and morphological changes.

Main Results:

• Treatment of cells with Vibrio cholerae neuraminidase rendered them resistant to Sendai virus infection.
• Endogenous receptor replacement occurred slowly, with maximal infection levels observed within 6 hours.
• Sialylation with CMP-sialic acid and beta-galactoside alpha 2,3-sialyltransferase restored full susceptibility to infection.
• Sialylation with beta-galactoside alpha 2,6-sialyltransferase did not restore infectivity.

Conclusions:

• Specific sialyloligosaccharide structures are essential for Sendai virus infection.
• The NeuAc alpha 2,3Gal beta 1,3GalNAc sequence, elaborated by beta-galactoside alpha 2,3-sialytransferase, functions as a key receptor determinant for Sendai virus.
• These findings elucidate the specific molecular requirements for paramyxovirus entry into host cells.