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Low pH-induced conformational change of rubella virus envelope proteins

S Katow1, A Sugiura

  • 1Department of Measles Virus, National Institute of Health, Tokyo, Japan.

Insights

Low pH triggers rubella virus-infected cell fusion by altering viral glycoproteins. This conformational change reduces virus infectivity and haemagglutination, mimicking endosomal entry.

Area of Science:

  • Virology
  • Cell Biology
  • Biochemistry

Background:

  • Rubella virus causes significant human disease.
  • Viral entry into host cells is a critical step in infection.
  • Understanding virus-host interactions is key to developing antiviral strategies.

Purpose of the Study:

  • To investigate the effect of acidic pH on rubella virus structure and function.
  • To elucidate the mechanism of rubella virus-induced cell fusion.
  • To determine if low pH-induced changes mimic natural viral entry processes.

Main Methods:

  • Treatment of rubella virus-infected cells with low pH buffers.
  • Exposure of purified rubella virus to acidic pH (pH 5).
  • Analysis of viral infectivity, haemagglutinating activity, and glycoprotein conformational changes using proteolytic digestion and liposome-binding assays.

Main Results:

  • Brief exposure to pH below 6.0 induced fusion of rubella virus-infected cells.
  • Exposure to pH 5 caused irreversible conformational changes in E1 and E2 glycoproteins.
  • These changes led to reduced viral infectivity and haemagglutination, altered protease resistance, and induced liposome-binding activity.

Conclusions:

  • Acidic pH induces rubella virus fusion by altering viral envelope glycoproteins.
  • The observed changes in viral structure and function at low pH are consistent with events during endocytosis.
  • This study provides insights into the molecular mechanisms of rubella virus entry and cell fusion.

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