scholarly journals Role for cysteine residues in the in vivo folding and assembly of the phage P22 tailspike

2001 ◽  
Vol 10 (2) ◽  
pp. 397-410 ◽  
Author(s):  
Cameron Haase-Pettingell ◽  
Scott Betts ◽  
Stephen W. Raso ◽  
Lisa Stuart ◽  
Anne Robinson ◽  
...  
Keyword(s):  
Cysteine Residues ◽  
Phage P22 ◽  
P22 Tailspike

Identification of novel α-gliadin genes

Genome ◽  
2011 ◽  
Vol 54 (3) ◽  
pp. 244-252 ◽  
Author(s):  
Peng-Fei Qi ◽  
Yu-Ming Wei ◽  
Qing Chen ◽  
Thérèse Ouellet ◽  
Jia Ai ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Triticum Aestivum L ◽  
Protein Band ◽  
Cysteine Residues ◽  
Disulphide Bonds ◽  
Chain Extenders ◽  
Domain I ◽  
Unique Domain

Ten novel α-gliadin genes (Gli-ta, Gli-turg1, Gli-turg2, Gli-turg3, Gli-turg4, Gli-turg5, Gli-turg6, Gli-cs1, Gli-cs2, and Gli-cs3) with unique characteristics were isolated from wheat ( Triticum aestivum L.), among which Gli-cs1, Gli-cs2, Gli-cs3, and Gli-turg6 were pseudogenes. Gli-cs3 and nine other sequences were much larger and smaller, respectively, than the typical α-gliadins. This variation was caused by insertion or deletion of the unique domain I and a polyglutamine region, possibly the result of illegitimate recombination. Consequently, Gli-cs3 contained 10 cysteine residues, whereas there were 2 cysteine residues only in the other nine sequences. Gli-ta/Gli-ta-like α-gliadin genes are normally expressed during the development of seeds. SDS–PAGE analysis showed that in-vitro-expressed Gli-ta could form intermolecular disulphide bonds and could be chain extenders. A protein band similar in size to Gli-ta has been observed in seed extracts, and mass spectrometry results confirm that the band contains small molecular mass α-gliadins, which is a characteristic of the novel α-gliadins. Mass spectrometry results also indicated that the two cysteine residues of Gli-ta/Gli-ta-like proteins participated in the formation of intermolecular disulphide bonds in vivo.

Identification of oxidized cysteine residues in signaling proteins in vivo

2018 ◽  
Vol 120 ◽  
pp. S126
Author(s):  
Zamorano Natalia ◽  
Fortin Audray ◽  
Chartier Stéfany ◽  
Grandvaux Nathalie
Keyword(s):  
Cysteine Residues ◽  
Signaling Proteins

scholarly journals Modification of Cysteine Residues In Vitro and In Vivo Affects the Immunogenicity and Antigenicity of Major Histocompatibility Complex Class I–restricted Viral Determinants

1999 ◽  
Vol 189 (11) ◽  
pp. 1757-1764 ◽  
Author(s):  
Weisan Chen ◽  
Jonathan W. Yewdell ◽  
Rodney L. Levine ◽  
Jack R. Bennink
Keyword(s):  
Influenza Virus ◽  
Posttranslational Modifications ◽  
Synthetic Peptides ◽  
Influenza Virus Infection ◽  
Lymphocytic Choriomeningitis ◽  
Reducing Agents ◽  
Cysteine Residues ◽  
T Cell Lines

In studying the subdominant status of two cysteine-containing influenza virus nuclear protein (NP) determinants (NP39–47 and NP218–226) restricted by H-2Kd, we found that the antigenicity of synthetic peptides was enhanced 10–100-fold by treatment with reducing agents, despite the fact that the affinity for Kd was not enhanced. Reducing agents also markedly enhanced the immunogenicity of cysteine-containing peptides, as measured by propagation of long-term T cell lines in vitro. Similar enhancing effects were obtained by substituting cysteine with alanine or serine in the synthetic peptides, demonstrating that sulfhydryl modification of cysteine is responsible for the impaired antigenicity and immunogenicity of NP39–47 and NP218–226. We found similar effects for two widely studied, cysteine-containing peptides from lymphocytic choriomeningitis virus. The major modifications of cysteine-containing synthetic peptides are cysteinylation and dimerization occurring through cysteine residues. We demonstrate that both of these modifications occur in cells synthesizing a cytosolic NP218–226 minigene product and, further, that T cells specific for cysteinylated NP218–226 are induced by influenza virus infection in mice, demonstrating that this modification occurs in vivo. These findings demonstrate that posttranslational modifications affect the immunogenicity and antigenicity of cysteine-containing viral peptides and that this must be considered in studying the status of such peptides in immunodominance hierarchies.

Enrichment of oxidised peptides of oxidised allows identification of oxidized cysteine residues in signaling proteins in vivo

2018 ◽  
Vol 128 ◽  
pp. S60
Author(s):  
Natalia Zamorano ◽  
Nathalie Grandvaux ◽  
Audray Fortin ◽  
Stéfany Chartier
Keyword(s):  
Cysteine Residues ◽  
Signaling Proteins

Secondary structure and thermostability of the phage P22 tailspike

1988 ◽  
Vol 199 (3) ◽  
pp. 491-502 ◽  
Author(s):  
Donna Sargent ◽  
James M. Benevides ◽  
Myeong-Hee Yu ◽  
Jonathan King ◽  
George J. Thomas
Keyword(s):  
Secondary Structure ◽  
Phage P22 ◽  
P22 Tailspike

Chemical chaperone-mediated protein folding: stabilization of P22 tailspike folding intermediates by glycerol

2007 ◽  
Vol 388 (8) ◽  
pp. 797-804 ◽  
Author(s):  
Rajesh Mishra ◽  
Rajiv Bhat ◽  
Robert Seckler
Keyword(s):  
Temperature Sensitive ◽  
Permissive Temperature ◽  
Chemical Chaperone ◽  
Preferential Hydration ◽  
Denatured State ◽  
Folding Intermediates ◽  
Fluorescence Measurements ◽  
Phage P22 ◽  
The Stability ◽  
P22 Tailspike

Abstract Polyol co-solvents such as glycerol increase the thermal stability of proteins. This has been explained by preferential hydration favoring the more compact native over the denatured state. Although polyols are also expected to favor aggregation by the same mechanism, they have been found to increase the folding yields of some large, aggregation-prone proteins. We have used the homotrimeric phage P22 tailspike protein to investigate the origin of this effect. The folding of this protein is temperature-sensitive and limited by the stability of monomeric folding intermediates. At non-permissive temperature (≥35°C), tailspike refolding yields were increased significantly in the presence of 1–4 m glycerol. At low temperature, tailspike refolding is prevented when folding intermediates are destabilized by the addition of urea. Glycerol could offset the urea effect, suggesting that the polyol acts by stabilizing crucial folding intermediates and not by increasing solvent viscosity. The stabilization effect of glycerol on tailspike folding intermediates was confirmed in experiments using a temperature-sensitive folding mutant protein, by fluorescence measurements of subunit folding kinetics, and by temperature up-shift experiments. Our results suggest that the chemical chaperone effect of polyols observed in the folding of large proteins is due to preferential hydration favoring structure formation in folding intermediates.

scholarly journals Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.

1996 ◽  
Vol 93 (20) ◽  
pp. 10584-10588 ◽  
Author(s):  
S. Steinbacher ◽  
U. Baxa ◽  
S. Miller ◽  
A. Weintraub ◽  
R. Seckler ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Antigen Receptors ◽  
O Antigen ◽  
Phage P22 ◽  
P22 Tailspike ◽  
Tailspike Protein

scholarly journals An essential serotype recognition pocket on phage P22 tailspike protein forces Salmonella enterica serovar Paratyphi A O-antigen fragments to bind as nonsolution conformers

Glycobiology ◽  
2013 ◽  
Vol 23 (4) ◽  
pp. 486-494 ◽  
Author(s):  
Dorothee Andres ◽  
Ulrich Gohlke ◽  
Nina K Broeker ◽  
Stefan Schulze ◽  
Wolfgang Rabsch ◽  
...  
Keyword(s):  
Salmonella Enterica ◽  
O Antigen ◽  
Phage P22 ◽  
P22 Tailspike ◽  
Tailspike Protein

scholarly journals Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain

1993 ◽  
Vol 215 (3) ◽  
pp. 653-661 ◽  
Author(s):  
Martina DANNER ◽  
Albert FUCHS ◽  
Stefan MILLER ◽  
Robert SECKLER
Keyword(s):  
Binding Domain ◽  
Phage P22 ◽  
P22 Tailspike

scholarly journals Expression of normal and truncated forms of human endoglin

1999 ◽  
Vol 339 (3) ◽  
pp. 579-588 ◽  
Author(s):  
Ulla RAAB ◽  
Beatriz VELASCO ◽  
Pedro LASTRES ◽  
Ainhoa LETAMENDÍA ◽  
Carmela CALÉS ◽  
...  
Keyword(s):  
Surface Protein ◽  
Recombinant Vaccinia Virus ◽  
Expression Vectors ◽  
Soluble Form ◽  
Cysteine Residues ◽  
Hereditary Haemorrhagic Telangiectasia ◽  
Coding Region ◽  
Transmembrane Glycoprotein

Endoglin is a transmembrane glycoprotein 633 residues in length expressed at the surface of endothelial cells as a disulphide-linked homodimer; the specific cysteine residues involved in endoglin dimerization are unknown. Mutations in the coding region of the endoglin gene are responsible for hereditary haemorrhagic telangiectasia type 1 (HHT1), a dominantly inherited vascular disorder. Many of these mutations, if translated, would lead to truncated forms of the protein. It is therefore of interest to assess the protein expression of different truncated forms of endoglin. Infections in vitro or in vivo with recombinant vaccinia virus, as well as transient transfections with expression vectors, were used to express normal and truncated forms of endoglin. Truncated mutants could be classified into three different groups: (1) those that did not produce stable transcripts; (2) those that produced stable transcripts but did not secrete the protein; and (3) those that secreted a soluble dimeric protein. This is the first time that a recombinant truncated form of endoglin has been found to be expressed in a soluble form. Because a chimaeric construct encoding the N-terminal sequence of platelet/endothelial cell adhesion molecule (PECAM-1) antigen fused to residues Ile281-Ala658 of endoglin also yielded a dimeric surface protein, these results suggest that cysteine residues contained within the fragment Cys330-Cys412 are involved in disulphide bond formation. Infection with vaccinia recombinants encoding an HHT1 mutation did not affect the expression of the normal endoglin, and did not reveal an association of the recombinant soluble form with the transmembrane endoglin, supporting a haploinsufficiency model for HHT1.

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