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Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
09:08

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Structural and mechanistic studies of measles virus illuminate paramyxovirus entry

Richard K Plemper1, Melinda A Brindley, Ronald M Iorio

  • 1Department of Pediatrics, Emory University School of Medicine, Atlanta, Georgia, United States of America. rplempe@emory.edu

Plos Pathogens
|June 10, 2011
PubMed

Insights

Measles virus (MeV) uses attachment (H) and fusion (F) proteins for cell entry. New structural data clarifies how H protein binding triggers F protein changes, advancing understanding of this highly infectious virus.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Measles virus (MeV) is a highly infectious paramyxovirus causing significant global pediatric morbidity and mortality.
  • Viral entry into host cells is crucial for MeV infection, mediated by envelope glycoproteins: attachment (H) and fusion (F) proteins.
  • The precise molecular mechanisms of MeV cell entry, particularly how receptor binding by H triggers F protein conformational changes, remain incompletely understood.

Purpose of the Study:

  • To review recent advances in understanding the molecular mechanisms of Measles virus (MeV) cell entry.
  • To elucidate the organization of functional paramyxovirus fusion complexes and the role of attachment protein receptor binding.
  • To contextualize these findings within the broader entry strategies of the paramyxovirus family.

Main Methods:

  • Analysis of recently reported crystal structures of the MeV attachment (H) protein in complex with cellular receptors CD46 or SLAM.
  • Integration of data from newly developed functional assays investigating MeV entry mechanisms.
  • Comparative review of entry strategies across different paramyxovirus family members.

Main Results:

  • Recent structural studies have illuminated the molecular interactions between the MeV attachment (H) protein and its receptors (CD46, SLAM).
  • New functional assays provide insights into the conformational rearrangements of the fusion (F) protein triggered by H protein receptor engagement.
  • These advances offer a clearer picture of the fundamental principles governing MeV cell entry.

Conclusions:

  • Recent structural and functional studies have significantly advanced the molecular understanding of Measles virus (MeV) entry.
  • The findings clarify how attachment protein receptor binding initiates fusion protein conformational changes, essential for viral entry.
  • This improved knowledge contributes to understanding paramyxovirus entry mechanisms and potential therapeutic targets.

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