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Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV1 Envelope gp120 Protein
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Effect of Glycosylation on an Immunodominant Region in the ~ Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein Jianhui Tian , # 1, 2 Cesar A. López , # 1 Cynthia A. Derdeyn , 3 Morris S. Jones , 4 Abraham Pinter , 5 Bette Korber , 1 and S. Gnanakaran 1, *
Effect of Glycosylation on an Immunodominant Region in the ~ RESEARCH ARTICLE Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein Jianhui Tian1,2☯, Cesar A. Lo´ pez1☯, Cynthia A. Derdeyn3, Morris S. Jones4, Abraham Pinter5, Bette Korber1, S. Gnanakaran1* 1 Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, New Mexico,
Effect of Glycosylation on an Immunodominant Region in the ~ Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein. Jianhui Tian , Los Alamos National Laboratory Cesar A. López , Los Alamos National Laboratory
(PDF) Effect of Glycosylation on an Immunodominant Region ~ Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein October 2016 PLoS Computational Biology 12(10)
(PDF) Figure S1 - ResearchGate ~ Heavy glycosylation of the envelope (Env) surface subunit, gp120, is a key adaptation of HIV-1; however, the precise effects of glycosylation on the folding, conformation and dynamics of this .
Common helical V1V2 conformations of HIV-1 Envelope expose ~ The α4β7 integrin is a non-essential HIV-1 adhesion receptor, bound by the gp120 V1V2 domain, facilitating rapid viral dissemination into gut-associated lymphoid tissues. Antibodies blocking .
How Hydrophobicity and the Glycosylation Site of Glycans ~ Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein. PLOS Computational Biology 2016 , 12 (10) , e1005094.
Chemical Synthesis of Highly Congested gp120 V1V2 N ~ Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein. PLOS Computational Biology 2016, 12 (10) , e1005094. DOI: 10.1371/journal.pcbi.1005094. Larissa Krasnova, Chi-Huey Wong. Exploring human glycosylation for better therapies.
Antigenicity and immunogenicity of HIV-1 gp140 with ~ The carbohydrate moieties on HIV-1 envelope glycoprotein (Env) act as shields to mask conserved neutralizing epitopes, while the hyperimmunogenic variable regions are immunodominant in inducing non-neutralizing antibodies, representing the major challenge for using Env as a vaccine candidate to induce broadly neutralizing antibodies (bNAbs).
Role of glycosylation in nucleating protein folding and ~ Glycosylation constitutes one of the most common, ubiquitous and complex forms of post-translational modification. It commences with the synthesis of the protein and plays a significant role in deciding its folded state, oligomerization and thus its function. Recent studies have demonstrated that N-linked glycans help proteins to fold as the stability and folding kinetics are altered with the .
Effects of glycosylation on antigenicity and ~ virus (HIV) gp120 envelope glycoprotein, proper expression of confor-mational epitopesis dependent on the integrity and presence of carbo-hydratemoieties(Haigwoodetal.,1992),sincefullyglycosylatedgp120 was found to present neutralizing epitopes more effectively than the nonglycosylated form of the envelope protein (Haigwood et al., 1992).
HIV-1 Envelope Glycoprotein Variable Loops Are ~ HIV-1 envelope (Env) glycoprotein is a trimer of heterodimer of gp120 and gp41, and derives from a trimeric glycoprotein precursor, gp160. Gp120 contains five conserved regions that are interspersed with 5 variable loop regions (V1–V5). Env variations in variable loop length and amino acid composition may associate with virus pathogenesis, virus sensitivity to neutralizing antibodies (nAbs .
Completeness of HIV-1 Envelope Glycan Shield at ~ Wagh et al. show that transmitted viruses with more intact glycan shields are correlated with development of neutralization breadth in HIV-1-infected individuals. This is consistent with previous findings that glycan holes in Env immunogens are targeted by strain-specific neutralizing responses, and suggests that immunogens with intact glycan shields may be advantageous.
All-atom virus simulations - ScienceDirect ~ Another well-studied envelope protein is the human immunodeficiency virus type 1 (HIV-1) envelope (Env) trimer (Figures 1b and 2 d), which mediates cellular adhesion and membrane fusion. All-atom MD simulations have been employed to characterize the conformational properties of Env, particularly its V3 variable domain, a critical determinant of .
Vaccine-induced V1V2-specific antibodies control and or ~ Conformational complexity of V1V2. In HIV, the V1V2 domain, like the rest of gp120, exhibits marked conformational flexibility. The V1V2 domain serves as the ‘trimer association domain’ at the apex of the closed trimeric Env, but the V1V2 domain of each of the three gp120 protomers opens out when gp120 interacts with CD4 [13–15,16 ].The C-strand of V2, composed of amino acids (AAs) 170 .
Envelope Deglycosylation Enhances Antigenicity of HIV-1 ~ Author Summary Critical to the design of an effective HIV-1 vaccine that will induce long-lasting broadly neutralizing antibodies is to understand why broad neutralizing antibodies are not induced. One hypothesis is that there are “holes” in the naïve B cell repertoires for unmutated B cell receptors that can bind to HIV-1 envelope (Env) neutralizing epitopes.
Evolution Rescues Folding of Human Immunodeficiency Virus ~ Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein 7 October 2016 / PLOS Computational Biology, Vol. 12, No. 10 Several N-Glycans on the HIV Envelope Glycoprotein gp120 Preferentially Locate Near Disulphide Bridges and Are Required for Efficient Infectivity and Virus Transmission
Effect of glycosylation on antibody function: implications ~ Effect of glycosylation on antibody function: implications for genetic engineering Ann Wright and Sherie L. Morrison Antibodies are able to both bind antigens and trigger the responses that eliminate them from circulation. All antibodies are glycosylated at conserved positions in their
Structure and Mutagenesis of Neural Cell Adhesion Molecule ~ Effect of glycosylation on an immunodominant region in the V1V2 variable domain of the HIV-1 envelope gp120 protein. Journal Article Tian, Jianhui; Lopez, . we focused on an antigenic peptide fragment from a disulfide bridge-bounded region spanning the V1 and V2 hyper-variable domains of HIV-1 gp120.
UvA-DARE (Digital Academic Repository) Improving HIV-1 ~ epitopes of the HIV-1 Env protein, variable domains were removed. Several studies have investigated removal of the V3 or V4 region, but this resulted in a total loss of Env function and virus infectivity (40,42-45). Deletion of the V1V2 variable domain also results in a
Sequence Note: Rapid Sequon Evolution in Human ~ Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein 7 October 2016 / PLOS Computational Biology, Vol. 12, No. 10 gag and env Sequences of an A/G/H Recombinant from a Zairian HIV Type 1 Isolate
Predominant envelope variable loop 2-specific and gp120 ~ The initial envelope (Env)-specific antibody response in acutely HIV-1-infected individuals and simian immunodeficiency virus (SIV)-infected rhesus monkeys (RMs) is dominated by non-neutralizing antibodies targeting Env gp41. In contrast, natural primate SIV hosts, such as African green monkeys (AGMs), develop a predominant Env gp120-specific antibody response to SIV infection.