scholarly journals Removal of the membrane penetration error from triaxial data

2020 ◽  
Vol 2 ◽  
pp. 1-None
Author(s):  
Andrzej Niemunis ◽  
Lukas Knittel
Keyword(s):  
Membrane Penetration

scholarly journals Membrane penetration of bovine factor V and Va detected by labeling with 5-iodonaphthalene-1-azide.

1987 ◽  
Vol 262 (5) ◽  
pp. 1935-1937
Author(s):  
M.F. Lecompte ◽  
S. Krishnaswamy ◽  
K.G. Mann ◽  
M.E. Nesheim ◽  
C. Gitler
Keyword(s):  
Factor V ◽  
Membrane Penetration ◽  
Bovine Factor

Membrane Penetration in Triaxial Tests

1982 ◽  
Vol 108 (2) ◽  
pp. 305-310
Author(s):  
K.V. Ramana ◽  
V.S. Raju
Keyword(s):  
Triaxial Tests ◽  
Membrane Penetration

scholarly journals Putative Autocleavage of Outer Capsid Protein μ1, Allowing Release of Myristoylated Peptide μ1N during Particle Uncoating, Is Critical for Cell Entry by Reovirus

2004 ◽  
Vol 78 (16) ◽  
pp. 8732-8745 ◽  
Author(s):  
Amy L. Odegard ◽  
Kartik Chandran ◽  
Xing Zhang ◽  
John S. L. Parker ◽  
Timothy S. Baker ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Structural Changes ◽  
General Mechanism ◽  
Membrane Penetration ◽  
Outer Capsid Protein ◽  
Core Proteins ◽  
Peptide Release ◽  
Outer Capsid

ABSTRACT Several nonenveloped animal viruses possess an autolytic capsid protein that is cleaved as a maturation step during assembly to yield infectious virions. The 76-kDa major outer capsid protein μ1 of mammalian orthoreoviruses (reoviruses) is also thought to be autocatalytically cleaved, yielding the virion-associated fragments μ1N (4 kDa; myristoylated) and μ1C (72 kDa). In this study, we found that μ1 cleavage to yield μ1N and μ1C was not required for outer capsid assembly but contributed greatly to the infectivity of the assembled particles. Recoated particles containing mutant, cleavage-defective μ1 (asparagine → alanine substitution at amino acid 42) were competent for attachment; processing by exogenous proteases; structural changes in the outer capsid, including μ1 conformational change and σ1 release; and transcriptase activation but failed to mediate membrane permeabilization either in vitro (no hemolysis) or in vivo (no coentry of the ribonucleotoxin α-sarcin). In addition, after these particles were allowed to enter cells, the δ region of μ1 continued to colocalize with viral core proteins in punctate structures, indicating that both elements remained bound together in particles and/or trapped within the same subcellular compartments, consistent with a defect in membrane penetration. If membrane penetration activity was supplied in trans by a coinfecting genome-deficient particle, the recoated particles with cleavage-defective μ1 displayed much higher levels of infectivity. These findings led us to propose a new uncoating intermediate, at which particles are trapped in the absence of μ1N/μ1C cleavage. We additionally showed that this cleavage allowed the myristoylated, N-terminal μ1N fragment to be released from reovirus particles during entry-related uncoating, analogous to the myristoylated, N-terminal VP4 fragment of picornavirus capsid proteins. The results thus suggest that hydrophobic peptide release following capsid protein autocleavage is part of a general mechanism of membrane penetration shared by several diverse nonenveloped animal viruses.

scholarly journals Lipid Membrane Penetration Forces from AFM Force Spectroscopy

2009 ◽  
Vol 96 (3) ◽  
pp. 389a
Author(s):  
Elizabeth A. Hager-Barnard ◽  
Benjamin D. Almquist ◽  
Nicholas A. Melosh
Keyword(s):  
Lipid Membrane ◽  
Force Spectroscopy ◽  
Membrane Penetration
Sign in / Sign up

Export Citation Format

Share Document