Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Virus versus antibody

P M Colman1

  • 1Biomolecular Research Institute, 343 Royal Parade, Parkville, Victoria 3052, Australia. peter.colman@mel.dbe.csiro.au

Structure (London, England : 1993)
|May 15, 1997
PubMed
Summary
This summary is machine-generated.

Viral protein variation enables reinfection but may not be constrained by receptor binding needs. Fundamental protein characteristics suggest flexibility in viral evolution and host interactions.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Crystal structure of Bax bound to the BH3 peptide of Bim identifies important contacts for interaction.

Cell death & disease·2015
Same author

Variola virus F1L is a Bcl-2-like protein that unlike its vaccinia virus counterpart inhibits apoptosis independent of Bim.

Cell death & disease·2015
Same author

How antibodies recognize virus proteins.

Immunology today·2014
Same author

Bax activation by Bim?

Cell death and differentiation·2009
Same author

EGL-1 BH3 mutants reveal the importance of protein levels and target affinity for cell-killing potency.

Cell death and differentiation·2008
Same author

Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands.

Cell death and differentiation·2008
Same journal

Meet the author: Stephen Brohawn.

Structure (London, England : 1993)·2026
Same journal

Tetraspanins bring Norrin into focus: Structural insights into ligand-specific Wnt signaling.

Structure (London, England : 1993)·2026
Same journal

Uncovering subtype-selective activation of the K<sub>Ca</sub>3.1 channel by SKA-111.

Structure (London, England : 1993)·2026
Same journal

Identification and structure determination of a type III-Bv CRISPR complex that post-translationally modifies an associated toxin.

Structure (London, England : 1993)·2026
Same journal

Cryo-EM structure of the Arabidopsisthaliana ribosome in translating and non-translating states.

Structure (London, England : 1993)·2026
Same journal

Multifaceted effects of N-glycosylation on amyloidogenic κ light chains in AL amyloidosis.

Structure (London, England : 1993)·2026
See all related articles

Area of Science:

  • Virology
  • Molecular Biology
  • Protein Dynamics

Background:

  • Animal viruses exhibit protein variation, enabling repeated host infections.
  • Maintaining critical viral functions, such as cellular receptor engagement, typically constrains this variation.

Purpose of the Study:

  • To investigate the extent to which protein variation in animal viruses is constrained by the need to maintain essential functions.
  • To explore the role of fundamental protein characteristics and interactions in viral adaptation.

Main Methods:

  • Analysis of viral protein structures and functions.
  • Computational modeling of protein-protein interactions.
  • Review of existing literature on viral evolution and host-pathogen dynamics.

Related Experiment Videos

Main Results:

  • Viral protein variation is less constrained than previously assumed.
  • Fundamental properties of proteins and their interactions allow for significant adaptability.
  • Receptor engagement may not be a primary limiting factor for viral protein evolution.

Conclusions:

  • The inherent nature of proteins and their interactions provides substantial flexibility for viral evolution.
  • Viruses may possess greater adaptive potential for reinfection and host interaction than currently recognized.