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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Alphavirus Transducing System: Tools for Visualizing Infection in Mosquito Vectors
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A novel system for visualizing alphavirus assembly.

J Jordan Steel1, Brian J Geiss2

  • 1Department of Microbiology, Immunology, and Pathology, Colorado State University, Fort Collins, CO 80523, USA.

Journal of Virological Methods
|July 1, 2015
PubMed
Summary
This summary is machine-generated.

Researchers developed a new live-cell imaging system to visualize alphavirus assembly. This tool tracks capsid and E2 protein interactions, aiding the study of virus formation and potential inhibitors.

Keywords:
AlphavirusFluorescence microscopySindbisVirus budding

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Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Alphaviruses are enveloped RNA viruses crucial to understand for their pathogenic potential.
  • Viral assembly, particularly alphavirus virion formation, is a complex process occurring at the cellular plasma membrane.
  • Existing methods for studying viral assembly in live cells have limitations.

Purpose of the Study:

  • To develop and validate a novel bimolecular fluorescence complementation (BiFC) system for visualizing alphavirus intracellular assembly in real-time.
  • To investigate the subcellular localization and association of alphavirus capsid and E2 glycoproteins during virion formation.
  • To establish a tool for identifying potential inhibitors of alphavirus particle production.

Main Methods:

  • Development of a BiFC system by fusing Venus fluorescent protein fragments (VN- and VC-) to the Sindbis virus capsid protein.
  • Expression of fluorescently tagged capsid and E2 glycoproteins in live cells.
  • Utilizing mutations in the capsid autoprotease active site to study polyprotein processing effects.
  • Incorporating mCherry fluorescent protein into the E2 glycoprotein for co-localization studies.

Main Results:

  • The BiFC system successfully visualized fluorescent capsid-like structures associating with the plasma membrane in the absence of viral genomes.
  • Mutation of the capsid autoprotease active site disrupted polyprotein processing and altered capsid protein localization.
  • Co-expression of mCherry-tagged E2 glycoprotein revealed its localization and close association with capsid proteins at the plasma membrane.
  • The developed system demonstrated its utility in studying alphavirus protein interactions during assembly.

Conclusions:

  • The developed BiFC system is a valuable tool for live-cell imaging of alphavirus assembly dynamics.
  • This system allows for real-time observation of capsid and E2 glycoprotein interactions at the plasma membrane.
  • The tool has potential applications in screening for antiviral compounds that disrupt alphavirus virion formation.