scholarly journals Interactions between Sindbis virus RNAs and a 68 amino acid derivative of the viral capsid protein further defines the capsid binding site

1994 ◽  
Vol 22 (5) ◽  
pp. 780-786 ◽  
Author(s):  
Barbara Weiss ◽  
Ute Geigenmüller-Gnirke ◽  
Sondra Schlesinger
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Capsid Protein ◽  
Acid Derivative ◽  
Sindbis Virus ◽  
Amino Acid Derivative ◽  
Viral Capsid ◽  
Viral Capsid Protein

scholarly journals Determination of encephalomyocarditis viral diabetogenicity by a putative binding site of the viral capsid protein

Diabetes ◽  
1998 ◽  
Vol 47 (4) ◽  
pp. 576-582 ◽  
Author(s):  
H. S. Jun ◽  
Y. Kang ◽  
H. S. Yoon ◽  
K. H. Kim ◽  
A. L. Notkins ◽  
...  
Keyword(s):  
Binding Site ◽  
Capsid Protein ◽  
Viral Capsid ◽  
Viral Capsid Protein ◽  
Putative Binding Site

scholarly journals Population Genomics of GII.4 Noroviruses Reveal Complex Diversification and New Antigenic Sites Involved in the Emergence of Pandemic Strains

2019 ◽  
Author(s):  
Kentaro Tohma ◽  
Cara J. Lepore ◽  
Yamei Gao ◽  
Lauren A. Ford-Siltz ◽  
Gabriel I. Parra
Keyword(s):  
Amino Acid ◽  
Capsid Protein ◽  
Large Scale ◽  
Population Genomics ◽  
Viral Capsid ◽  
Viral Gastroenteritis ◽  
Viral Capsid Protein ◽  
Antigenic Sites ◽  
Capsid Protein Vp1

AbstractGII.4 noroviruses are a major cause of acute gastroenteritis. Their dominance has been partially explained by the continuous emergence of antigenically distinct variants. To gain insights on the mechanisms of viral emergence and population dynamics of GII.4 noroviruses, we performed large-scale genomics, structural, and mutational analyses of the viral capsid protein (VP1). GII.4 noroviruses exhibited a periodic replacement of predominant variants with accumulation of amino acid substitutions. Genomic analyses revealed (i) a large number (87%) of conserved residues; (ii) variable residues that map on the previously determined antigenic sites; and (iii) variable residues that map outside of the antigenic sites. Residues from the third pattern formed motifs on the surface of VP1, which suggested extensions of previously predicted and new uncharacterized antigenic sites. The role of two motifs (C and G) in the antigenic make-up of the GII.4 capsid protein was confirmed with monoclonal antibodies and carbohydrate blocking assays. Amino acid profiles from antigenic sites (A, C, D, E, and G) correlated with the circulation patterns of GII.4 variants, with two of them (C and G) containing residues (352, 357, 378) linked with the emergence of new GII.4 variants. Notably, the emergence of each variant was followed by a stochastic diversification with minimal changes at the antigenic sites that did not progress towards the next variant. This study provides a methodological framework for antigenic characterization of viruses, and expands our understanding of the dynamics of GII.4 noroviruses that could facilitate the design of cross-reactive vaccines.ImportanceNoroviruses are an important cause of viral gastroenteritis around the world. An obstacle delaying the development of norovirus vaccines is an inadequate understanding of the role of norovirus diversity in immunity. Using a population genomics approach, we identified new residues on the viral capsid protein (VP1) from GII.4 noroviruses, the predominant genotype, that appear to be involved in the emergence and antigenic topology of GII.4 variants. Careful monitoring of the substitutions in those residues involved in the diversification and emergence of new viruses could help in the early detection of future novel variants with pandemic potential. Therefore, this novel information on the antigenic diversification could facilitate GII.4 norovirus vaccine design.

Amino Acid Substitutions At Residue 207 of Viral Capsid Protein 1 (VP1) Confer Pleconaril Resistance in Coxsackievirus B3 (CVB3)

2011 ◽  
Vol 90 (2) ◽  
pp. A54-A55 ◽  
Author(s):  
Heike Braun ◽  
Vadim A. Makarov ◽  
Olga B. Riabova ◽  
Peter Wutzler ◽  
Michaela Schmidtke
Keyword(s):  
Amino Acid ◽  
Capsid Protein ◽  
Coxsackievirus B3 ◽  
Viral Capsid ◽  
Amino Acid Substitutions ◽  
Viral Capsid Protein

scholarly journals Population Genomics of GII.4 Noroviruses Reveal Complex Diversification and New Antigenic Sites Involved in the Emergence of Pandemic Strains

mBio ◽  
2019 ◽  
Vol 10 (5) ◽  
Author(s):  
Kentaro Tohma ◽  
Cara J. Lepore ◽  
Yamei Gao ◽  
Lauren A. Ford-Siltz ◽  
Gabriel I. Parra
Keyword(s):  
Amino Acid ◽  
Capsid Protein ◽  
Large Scale ◽  
Population Genomics ◽  
Viral Capsid ◽  
Viral Gastroenteritis ◽  
Viral Capsid Protein ◽  
Antigenic Sites ◽  
Capsid Protein Vp1

ABSTRACT GII.4 noroviruses are a major cause of acute gastroenteritis. Their dominance has been partially explained by the continuous emergence of antigenically distinct variants. To gain insights into the mechanisms of viral emergence and population dynamics of GII.4 noroviruses, we performed large-scale genomics, structural, and mutational analyses of the viral capsid protein (VP1). GII.4 noroviruses exhibited a periodic replacement of predominant variants with accumulation of amino acid substitutions. Genomic analyses revealed (i) a large proportion (87%) of conserved residues; (ii) variable residues that map on the previously determined antigenic sites; and (iii) variable residues that map outside the antigenic sites. Residues in the third pattern category formed motifs on the surface of VP1, which suggested extensions of previously predicted and new uncharacterized antigenic sites. The role of two motifs (C and G) in the antigenic makeup of the GII.4 capsid protein was confirmed with monoclonal antibodies and carbohydrate blocking assays. Amino acid profiles from antigenic sites (A, C, D, E, and G) correlated with the circulation patterns of GII.4 variants, with three of them (A, C, and G) containing residues (352, 357, 368, and 378) linked with the diversifying selective pressure on the emergence of new GII.4 variants. Notably, the emergence of each variant was followed by stochastic diversification with minimal changes that did not progress toward the next variant. This report provides a methodological framework for antigenic characterization of viruses and expands our understanding of the dynamics of GII.4 noroviruses and could facilitate the design of cross-reactive vaccines. IMPORTANCE Noroviruses are an important cause of viral gastroenteritis around the world. An obstacle delaying the development of norovirus vaccines is inadequate understanding of the role of norovirus diversity in immunity. Using a population genomics approach, we identified new residues on the viral capsid protein (VP1) from GII.4 noroviruses, the predominant genotype, that appear to be involved in the emergence and antigenic topology of GII.4 variants. Careful monitoring of the substitutions in those residues involved in the diversification and emergence of new viruses could help in the early detection of future novel variants with pandemic potential. Therefore, this novel information on the antigenic diversification could facilitate GII.4 norovirus vaccine design.

scholarly journals Inhibition of HIV-1 Maturation via Small-Molecule Targeting of the Amino-Terminal Domain in the Viral Capsid Protein

2017 ◽  
Vol 91 (9) ◽  
Author(s):  
Weifeng Wang ◽  
Jing Zhou ◽  
Upul D. Halambage ◽  
Kellie A. Jurado ◽  
Augusta V. Jamin ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Capsid Protein ◽  
Small Molecule ◽  
Single Amino Acid ◽  
Viral Capsid ◽  
Capsid Assembly ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Hiv 1

ABSTRACT The human immunodeficiency virus type 1 (HIV-1) capsid protein is an attractive therapeutic target, owing to its multifunctionality in virus replication and the high fitness cost of amino acid substitutions in capsids to HIV-1 infectivity. To date, small-molecule inhibitors have been identified that inhibit HIV-1 capsid assembly and/or impair its function in target cells. Here, we describe the mechanism of action of the previously reported capsid-targeting HIV-1 inhibitor, Boehringer-Ingelheim compound 1 (C1). We show that C1 acts during HIV-1 maturation to prevent assembly of a mature viral capsid. However, unlike the maturation inhibitor bevirimat, C1 did not significantly affect the kinetics or fidelity of Gag processing. HIV-1 particles produced in the presence of C1 contained unstable capsids that lacked associated electron density and exhibited impairments in early postentry stages of infection, most notably reverse transcription. C1 inhibited assembly of recombinant HIV-1 CA in vitro and induced aberrant cross-links in mutant HIV-1 particles capable of spontaneous intersubunit disulfide bonds at the interhexamer interface in the capsid lattice. Resistance to C1 was conferred by a single amino acid substitution within the compound-binding site in the N-terminal domain of the CA protein. Our results demonstrate that the binding site for C1 represents a new pharmacological vulnerability in the capsid assembly stage of the HIV-1 life cycle. IMPORTANCE The HIV-1 capsid protein is an attractive but unexploited target for clinical drug development. Prior studies have identified HIV-1 capsid-targeting compounds that display different mechanisms of action, which in part reflects the requirement for capsid function at both the efferent and afferent phases of viral replication. Here, we show that one such compound, compound 1, interferes with assembly of the conical viral capsid during virion maturation and results in perturbations at a specific protein-protein interface in the capsid lattice. We also identify and characterize a mutation in the capsid protein that confers resistance to the inhibitor. This study reveals a novel mechanism by which a capsid-targeting small molecule can inhibit HIV-1 replication.

Synthesis of amino acid derivative Schiff base copper(II) complexes by microwave and wet mechanochemical methods

2021 ◽  
Vol 98 (1) ◽  
pp. 100004
Author(s):  
Nao Otani ◽  
Tetsundo Furuya ◽  
Natsuki Katsuumi ◽  
Tomoyuki Haraguchi ◽  
Takashiro Akitsu
Keyword(s):  
Schiff Base ◽  
Amino Acid ◽  
Acid Derivative ◽  
Amino Acid Derivative

Resolution of racemic mixture of α-amino acid derivative through composite membrane

2011 ◽  
Vol 378 (1-2) ◽  
pp. 531-540 ◽  
Author(s):  
Kripal Singh ◽  
Pravin G. Ingole ◽  
Jayesh Chaudhari ◽  
Harshad Bhrambhatt ◽  
Amit Bhattacharya ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Derivative ◽  
Composite Membrane ◽  
Amino Acid Derivative ◽  
Racemic Mixture

scholarly journals Self-Assembly of Viral Capsid Protein and RNA Molecules of Different Sizes: Requirement for a Specific High Protein/RNA Mass Ratio

2011 ◽  
Vol 86 (6) ◽  
pp. 3318-3326 ◽  
Author(s):  
R. D. Cadena-Nava ◽  
M. Comas-Garcia ◽  
R. F. Garmann ◽  
A. L. N. Rao ◽  
C. M. Knobler ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Self Assembly ◽  
High Protein ◽  
Viral Capsid ◽  
Mass Ratio ◽  
Viral Capsid Protein ◽  
Rna Molecules

Expression of viral capsid protein antigen against Epstein-Barr virus in plastids ofNicotiana tabacum cv. SR1

2006 ◽  
Vol 94 (6) ◽  
pp. 1129-1137 ◽  
Author(s):  
Maggie Y.T. Lee ◽  
Yuanxiang Zhou ◽  
Raymond W.M. Lung ◽  
Mee-Len Chye ◽  
Wing-Kin Yip ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Epstein Barr Virus ◽  
Protein Antigen ◽  
Viral Capsid ◽  
Viral Capsid Protein ◽  
Barr Virus ◽  
Ofnicotiana Tabacum ◽  
Epstein Barr
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