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Related Concept Videos

COP Coated Vesicles00:59

COP Coated Vesicles

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Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
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Asymmetric Lipid Bilayer01:35

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Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
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Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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Surface Membrane Barriers01:18

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The skin and mucous membranes serve as the primary line of defense against pathogens by providing both physical and chemical protection. These barriers are essential in preventing the entry and establishment of microbes, thereby maintaining the integrity of the host.
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Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

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Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
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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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Related Experiment Video

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Visualization of HIV-1 Gag Binding to Giant Unilamellar Vesicle GUV Membranes
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Parvovirus B19 VLP recognizes globoside in supported lipid bilayers.

Waqas Nasir1, Jonas Nilsson1, Sigvard Olofsson2

  • 1Department of Clinical Chemistry and Transfusion Medicine, Sahlgrenska Academy, University of Gothenburg, Bruna Stråket 16, 413 45 Gothenburg, Sweden.

Virology
|June 4, 2014
PubMed
Summary

Human parvovirus B19 uses globoside (Gb4Cer) as a receptor. This study confirms Gb4Cer and Forssman glycosphingolipid binding by virus-like particles on cell membrane mimics, supporting Gb4Cer

Keywords:
CarbohydrateGlycanGlycobiologyGlycosphingolipidsParvovirus B19 virus-like particles

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Area of Science:

  • Virology
  • Biochemistry
  • Cell Biology

Background:

  • Globoside (Gb4Cer) is a proposed receptor for human parvovirus B19.
  • Direct interaction of parvovirus B19 with membrane-associated Gb4Cer remains debated.
  • Virus-like particles (VLPs) are used to study parvovirus B19 binding.

Purpose of the Study:

  • To characterize the binding of parvovirus B19 VLPs to glycosphingolipids.
  • To investigate VLP binding on thin-layer chromatograms (TLCs) and supported lipid bilayers (SLBs).
  • To validate Gb4Cer as a functional receptor for parvovirus B19.

Main Methods:

  • Parvovirus B19 VP1/VP2 VLPs were used.
  • Glycosphingolipid binding was assessed on TLCs.
  • VLP-glycosphingolipid interactions were analyzed within SLBs mimicking cell membranes.

Main Results:

  • VLP binding specificities were consistent between TLCs and SLBs.
  • Parvovirus B19 VLPs recognized both Gb4Cer and Forssman glycosphingolipid.
  • Binding occurred on SLBs, validating cell membrane mimicry.

Conclusions:

  • Gb4Cer and Forssman glycosphingolipid are recognized by parvovirus B19 VLPs.
  • Supported lipid bilayers effectively mimic cell membranes for VLP binding studies.
  • Findings support the role of Gb4Cer as a functional receptor for human parvovirus B19.