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Related Experiment Videos

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

Virology
|April 23, 2003
PubMed
Summary
This summary is machine-generated.

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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.

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:

Related Experiment Videos

  • 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.