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2 edition of Polypeptide changes in L-cell plasma membranes after reovirus infection found in the catalog.

Polypeptide changes in L-cell plasma membranes after reovirus infection

Mark Robert Coleman

Polypeptide changes in L-cell plasma membranes after reovirus infection

by Mark Robert Coleman

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  • 2 Currently reading

Published .
Written in English

    Subjects:
  • Reoviruses,
  • Membranes (Biology)

  • Edition Notes

    Statementby Mark R. Coleman
    The Physical Object
    Pagination45 leaves :
    Number of Pages45
    ID Numbers
    Open LibraryOL17845907M

    Plasma Membrane Reshaping during Endocytosis Is Revealed by Time-Resolved Electron Tomography Wanda Kukulski,1,2 Martin Schorb,1 Marko Kaksonen,1,2,* and John A.G. Briggs1,2,* 1Structural and Computational Biology Unit 2Cell Biology and Biophysics Unit European Molecular Biology Laboratory, Meyerhofstrasse 1, D Heidelberg, Germany. Cell-penetrating peptides (CPPs) are cationic peptides that are able to induce cellular uptake and delivery of large and hydrophilic molecules, that otherwise do not cross the plasma membrane of.

    Mammalian orthoreoviruses (called reoviruses here) are nonenveloped, icosahedral viruses consisting of two concentric protein shells—an outer capsid and inner core—that contain a genome of ten dsRNA segments [].The reovirus replication cycle is entirely cytoplasmic ().Following entry into the cells, the viral outer capsid is proteolytically cleaved in the late endosomes to form Cited by: 1. Clathrin-mediated endocytosis (CME) is an important entry pathway for viruses. Here, we applied click chemistry to covalently immobilize reovirus on surfaces to study CME during early host–pathogen interactions. To uncouple chemical and physical properties of viruses and determine their impact on CME initiation, we used the same strategy to covalently immobilize nanoparticles of different Cited by: 6.

    The interactions between peptides and lipids are of fundamental importance in the functioning of numerous membrane-mediated cellular processes including antimicrobial peptide action, hormone-receptor interactions, drug bioavailability across the blood-brain barrier and viral fusion processes. Moreover, a major goal of modern biotechnology is obtaining new potent pharmaceutical agents Cited by: Viroporins were first identified in , after the observation that a viral infection could induce changes in the permeability of the host cell plasma membrane [].This seminal work, and many others that followed, established the idea of viroporins as a protein family [].Viroporins play a key role in the virus life cycle; deletion of a viroporin-encoding gene from a viral genome drastically Cited by: 6.


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Polypeptide changes in L-cell plasma membranes after reovirus infection by Mark Robert Coleman Download PDF EPUB FB2

Although cell-cell fusion is an uncommon property of nonenveloped viruses, syncytium formation is associated with the replication cycle of numerous enveloped viruses, reflecting the presence of viral fusion proteins in the plasma membrane of virus-infected cells, a natural consequence of the assembly and release strategies of these by:   () Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image by:   Studies further suggest that cell-cell fusion mediated by the FAST proteins may contribute to rapid localized dissemination of the infection, followed by apoptosis-induced disruption of the syncytia, resulting in a burst of infectious-progeny-virus release (19, 21, 41).Cited by:   When infection is carried out with cells in culture, however, unmodified virions can attach, and endosomal proteases then strip off σ3.

μ1, exposed by σ3 removal, provides the membrane penetration by: Specific plasma membrane receptors for reovirus on rat pituitary cells in culture Article (PDF Available) in Journal of Clinical Investigation 72(2) September with 16 Reads.

Only the to kDa, virion-derived polypeptide should be present on infected cell surfaces and our results support this conclusion.

The analysis does not distinguish between vi- rion-derived kDa polypeptide and a polypeptide with a similar molecular weight, which was synthesized and then expressed on plasma membranes, after by: 9. Lane 1: uninfected cells; lanes cells labeled beginning at 9, 24, and 31 hr after infection.

and 31 hr after infection (lanes 3, 4). In stationary cultures of reovirus-infected L cells, synthesis of viral proteins, including a product of apparent molecular weight similar to pl4, was maximal at about 12 hr after infection (Jacobs and Samuel Cited by: Avian reovirus (ARV) infections characterised by severe arthritis, tenosynovitis, pericarditis, and depressed growth have become increasingly frequent in recent years.

Fig. Model of reovirus attachment to JAM-A on the cell surface. A ribbon-trace model of full-length T3D σ1, extending from a schematic virion, with the known structure of the C-terminus (Chappell et al.

) in tricolor and the prediction for the N-terminus in predicted SA-binding site (Chappell et al. ; Dermody et al. ) is marked with a by: Figure 1. Plasma membrane lipid and cholesterol distribution. (a) Pie charts showing the distribution of the main lipid headgroups and the levels of tail unsaturation in the inner and outer leaflets.

(b) A snapshot of the plasma membrane after 40 μs of simulation viewed on the outer leaflet. VIROL () The Synthesis of Sendai Virus Polypeptides in Infected Cells II.

Intracellular Distribution of Polypeptides ROBERT A. LAMB1 AND PURNELL W. CHOPPIN The Rockefeller University, New York, New York Accepted May 9, The intracellular distribution and the kinetics of association of Sendai virus poly- peptides with cytoplasmic fractions and plasma membranes Cited by: Amphipathic peptides are known to target and sometimes destabilize membranes, and this region of μ1 was previously suggested to be involved in membrane penetration during virus entry.

Based on these previous findings, we hypothesized that one mechanism by which μ1 induces apoptosis is by direct destabilization of intracellular by: 7. ConspectusThe structure–function relationship for a family of antimicrobial peptides (AMPs) from the skin of Australian tree frogs is discussed and compared with that of peptide toxins from bee and Australian scorpion venoms.

Although these membrane-active peptides induce a similar cellular fate by disrupting the lipid bilayer integrity, their lytic activity is achieved via different modes Cited by: The outer capsid of the nonenveloped mammalian reovirus contains trimers of the μ1 protein, each complexed with three copies of the protector protein σ3.

Conformational changes in μ1 following the proteolytic removal of σ3 lead to release of the myristoylated N-terminal cleavage fragment μ1N and ultimately to membrane by: Solution The lipid bilayer is the outer-most layer surrounding the cell.

Problem: What is the main function of the lipid bilayer. The lipid bilayer acts as a barrier between the inside and outside of the cell. It is highly impermeable and does not allow most molecules to freely pass through it into. Conformational changes in micro1 following the proteolytic removal of sigma3 lead to release of the myristoylated N-terminal cleavage fragment micro1N and ultimately to membrane penetration.

The lists with the most enriched proteins in zebrafish plasma at the progressive time points after SVCV infection can be found in Table 3, S1 and S2. Proteins showing the highest increments in relative abundance over non-infected controls were vitellogenins (Vtgs), coagulation factor XIII, the grass carp reovirus induced protein Gig2 Cited by: 2.

reovirus and thus study the effect of predetermined changes on the viral multiplication cycle [19 – 21]. More recently, high-throughput approaches have also been used to extensively look at the Author: Guy Lemay.

This Journal Full Site. Advanced Search. Log in; Register; Subscribe; Claim. Pathogenesis of Reovirus Infection. Authors; Authors and affiliations and Fields, B.N., b, Use of an aberrant polypeptide as a marker in three-factor crosses: Further evidence for W.D., and Lengyel, P.,Translation of in vitro synthesized reovirus mRNAs into proteins of the size of reovirus capsid proteins in a mouse L cell Cited by:.

Several arginine rich antimicrobial peptides can also form pores in lipid bilayers and bacterial cell membranes (25, 26). It is known that antimicrobial peptides are able to translocate across the bacterial plasma membrane in an energy-independent manner. Since CPPs also seem capable of translocation in an energy independent manner, they.Reovirus is under development as a therapeutic for numerous types of cancer.

In contrast to other oncolytic viruses, the safety and efficacy of reovirus have not been improved through genetic manipulation. Here, we tested the oncolytic capacity of recombinant strains (rs) of prototype reovirus laboratory strains T1L and T3D (rsT1L and rsT3D, respectively) in a panel of non-small cell lung Cited by: 6.The plasma membrane is made up primarily of a bilayer of phospholipids with embedded proteins, carbohydrates, glycolipids, and glycoproteins, and, in animal cells, cholesterol.

The amount of cholesterol in animal plasma membranes regulates the fluidity of the membrane and changes based on the temperature of the cell’s environment.