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Sin Nombre virus glycoprotein trafficking.

C F Spiropoulou¹, C S Goldsmith, T R Shoemaker

¹Special Pathogens Branch, Division of Viral and Rickettsial Diseases, National Center for Infectious Diseases, Centers for Disease Control and Prevention, Atlanta, GA 30333, USA. ccs8@cdc.gov

|April 23, 2003

Summary

Sin Nombre virus (SNV) glycoproteins primarily mature in the Golgi complex, unlike other New World hantaviruses. Researchers discovered a significant intracellular pool of SNV G1 protein in late endosomes-lysosomes.

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Area of Science:

Virology
Cell Biology
Molecular Biology

Background:

Sin Nombre virus (SNV) causes hantavirus pulmonary syndrome (HPS) in North America.
New World hantaviruses were thought to mature at the cell surface, differing from other Bunyaviridae family members.

Purpose of the Study:

To investigate the maturation and localization of SNV glycoproteins (G1 and G2).
To clarify the intracellular trafficking of SNV G1 and G2 proteins.

Main Methods:

Expression of SNV glycoproteins from a full-length GPC clone.
Analysis of SNV-infected cells.
Immunofluorescence microscopy using SNV G1-specific antibodies.
Subcellular localization studies.

Main Results:

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SNV G1 and G2 glycoproteins predominantly localized to the Golgi complex, similar to Old World hantaviruses.
SNV glycoproteins were also found at the cell surface at later time points.
G1, without G2, localized to the endoplasmic reticulum (ER).
A significant intracellular pool of G1 was identified in late endosomes-lysosomes in infected and transfected cells.

Conclusions:

SNV glycoproteins exhibit Golgi maturation, aligning with other Bunyaviridae.
The study reveals an unexpected intracellular localization of SNV G1 in late endosomes-lysosomes.
Findings challenge previous assumptions about New World hantavirus maturation pathways.