A Single Amino Acid Variation Within an Immunodominant AKR/Gross MuLV Cytotoxic T-Lymphocyte Epitope Leads to a Loss in Immunogenicity

1998 ◽  
Vol 11 (4) ◽  
pp. 197-213 ◽  
Author(s):  
VICTOR KIM ◽  
WILLIAM R. GREEN
Keyword(s):  
Amino Acid ◽  
T Lymphocyte ◽  
Cytotoxic T Lymphocyte ◽  
Single Amino Acid ◽  
Amino Acid Variation

Virus-specific cytotoxic T-lymphocyte responses select for amino-acid variation in simian immunodeficiency virus Env and Nef

10.1038/15224 ◽  
1999 ◽  
Vol 5 (11) ◽  
pp. 1270-1276 ◽  
Author(s):  
David T. Evans ◽  
David H. O'Connor ◽  
Peicheng Jing ◽  
John L. Dzuris ◽  
John Sidney ◽  
...  
Keyword(s):  
Amino Acid ◽  
Simian Immunodeficiency Virus ◽  
T Lymphocyte ◽  
Cytotoxic T Lymphocyte ◽  
Amino Acid Variation ◽  
Immunodeficiency Virus ◽  
Lymphocyte Responses

A single amino acid substitution improves the in vivo immunogenicity of the HPV16 oncoprotein E7(11–20) cytotoxic T lymphocyte epitope

Vaccine ◽  
2005 ◽  
Vol 23 (31) ◽  
pp. 4005-4010 ◽  
Author(s):  
Marco W.J. Schreurs ◽  
Esther W.M. Kueter ◽  
Kirsten B.J. Scholten ◽  
François A. Lemonnier ◽  
Chris J.L.M. Meijer ◽  
...  
Keyword(s):  
Amino Acid ◽  
T Lymphocyte ◽  
Amino Acid Substitution ◽  
Cytotoxic T Lymphocyte ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid

scholarly journals Single Amino Acid Variation Underlies Species-Specific Sensitivity to Amphibian Skin-Derived Opioid-like Peptides

2015 ◽  
Vol 22 (6) ◽  
pp. 764-775 ◽  
Author(s):  
Eyal Vardy ◽  
Maria F. Sassano ◽  
Andrew J. Rennekamp ◽  
Wesley K. Kroeze ◽  
Philip D. Mosier ◽  
...  
Keyword(s):  
Amino Acid ◽  
Single Amino Acid ◽  
Amphibian Skin ◽  
Amino Acid Variation ◽  
Specific Sensitivity ◽  
Species Specific

scholarly journals Cancer-related single amino acid variation prediction

2020 ◽  
Author(s):  
Jia Jun Liu ◽  
Chin Sheng Yu ◽  
Hsiao Wei Wu ◽  
Yu Jen Chang ◽  
Chih Peng Lin ◽  
...  
Keyword(s):  
Amino Acid ◽  
Single Amino Acid ◽  
Amino Acid Variation

scholarly journals Three Immunoproteasome-Associated Subunits Cooperatively Generate a Cytotoxic T-Lymphocyte Epitope of Epstein-Barr Virus LMP2A by Overcoming Specific Structures Resistant to Epitope Liberation

2006 ◽  
Vol 80 (2) ◽  
pp. 883-890 ◽  
Author(s):  
Yoshinori Ito ◽  
Eisei Kondo ◽  
Ayako Demachi-Okamura ◽  
Yoshiki Akatsuka ◽  
Kunio Tsujimura ◽  
...  
Keyword(s):  
T Lymphocyte ◽  
Epstein Barr Virus ◽  
Cytotoxic T Lymphocyte ◽  
Single Amino Acid ◽  
Extrinsic Factors ◽  
Α Subunit ◽  
Intrinsic Factors ◽  
Barr Virus ◽  
Cleavage Strength ◽  
Epstein Barr

ABSTRACT The precise roles of gamma interferon-inducible immunoproteasome-associated molecules in generation of cytotoxic T-lymphocyte (CTL) epitopes have yet to be fully elucidated. We describe here a unique epitope derived from the Epstein-Barr virus (EBV) latent membrane protein 2A (LMP2A) presented by HLA-A*2402 molecules. Generation of the epitope, designated LMP2A222-230, from the full-length protein requires the immunoproteasome subunit low-molecular-weight protein 7 (ip-LMP7) and the proteasome activator 28-α subunit and is accelerated by ip-LMP2, as revealed by gene expression experiments using an LMP2A222-230-specific CTL clone as a responder in enzyme-linked immunospot assays. The unequivocal involvement of all three components was confirmed by RNA interference gene silencing. Interestingly, the LMP2A222-230 epitope could be efficiently generated from incomplete EBV-LMP2A fragments that were produced by puromycin treatment or gene-engineered shortened EBV-LMP2A lacking some of its hydrophobic domains. In addition, epitope generation was increased by a single amino acid substitution from leucine to alanine immediately flanking the C terminus, this being predicted by a web-accessible program to increase the cleavage strength. Taken together, the data indicate that the generation of LMP2A222-230 is influenced not only by extrinsic factors such as immunoproteasomes but also by intrinsic factors such as the length of the EBV-LMP2A protein and proteasomal cleavage strength at specific positions in the source antigen.

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