scholarly journals Definition of the Primary Structure of Hepatitis B Virus (HBV) pre-S Hepatocyte Binding Domain Using Random Peptide Libraries

Virology ◽  
1997 ◽  
Vol 237 (2) ◽  
pp. 319-326 ◽  
Author(s):  
Felicity D'Mello ◽  
Charalambos D. Partidos ◽  
Michael W. Steward ◽  
Colin R. Howard
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Primary Structure ◽  
Binding Domain ◽  
Peptide Libraries ◽  
Random Peptide ◽  
B Virus ◽  
Random Peptide Libraries ◽  
Definition Of

scholarly journals A Novel DNA Vaccine Against SARS-CoV-2 Encoding a Chimeric Protein of Its Receptor-Binding Domain (RBD) Fused to the Amino-Terminal Region of Hepatitis B Virus preS1 With a W4P Mutation

2021 ◽  
Vol 12 ◽  
Author(s):  
Hyein Jeong ◽  
Yu-Min Choi ◽  
Hyejun Seo ◽  
Bum-Joon Kim
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Dna Vaccine ◽  
Receptor Binding ◽  
Chimeric Protein ◽  
Binding Domain ◽  
Terminal Region ◽  
Receptor Binding Domain ◽  
Enhanced Production ◽  
B Virus

A coronavirus SARS-CoV-2, which has caused the pandemic viral pneumonia disease COVID-19, significantly threatens global public health, highlighting the need to develop effective and safe vaccines against its infection. In this study, we developed a novel DNA vaccine candidate against SARS-CoV-2 by expressing a chimeric protein of its receptor-binding domain (RBD) fused to a 33-bp sequence (11 aa) from the hepatitis B virus (HBV) preS1 region with a W4P mutation (W4P-RBD) at the N-terminal region and evaluated its immunogenicity. In vitro transfection experiments in multiple cell lines demonstrated that W4P-RBD vs. wild-type RBD protein (W-RBD) led to enhanced production of IL-6 and TNFα at the transcription and translation levels, suggesting the adjuvant potential of N-terminal HBV preS1 sequences for DNA vaccines against SARS-CoV-2. W4P-RBD also led to enhanced production of IgG and IgA, which can neutralize and block SARS-CoV-2 infection in both blood sera and bronchoalveolar lavage (BAL) fluid from the lung in vaccinated mice. Additionally, W4P-RBD led to an enhanced T-cell-mediated cellular immune response under S1 protein stimulation. In summary, W4P-RBD led to robust humoral and cell-mediated immune responses against SARS-CoV-2 in vaccinated mice, highlighting its feasibility as a novel DNA vaccine to protect against SARS-CoV-2 infection.

scholarly journals Definition of a minimal optimal cytotoxic T-cell epitope within the hepatitis B virus nucleocapsid protein.

1993 ◽  
Vol 67 (4) ◽  
pp. 2376-2380 ◽  
Author(s):  
A Bertoletti ◽  
F V Chisari ◽  
A Penna ◽  
S Guilhot ◽  
L Galati ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
T Cell ◽  
Hepatitis B ◽  
Nucleocapsid Protein ◽  
Cell Epitope ◽  
Cytotoxic T Cell ◽  
T Cell Epitope ◽  
B Virus ◽  
Definition Of

scholarly journals Clarification Required for the Definition of Hepatitis B Virus Subgenotypes C1 and C2

Intervirology ◽  
2009 ◽  
Vol 52 (6) ◽  
pp. 321-322 ◽  
Author(s):  
Sang Hoon Ahn ◽  
Lilly Yuen ◽  
Peter Revill
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
B Virus ◽  
Definition Of

HEPATITIS B VIRUS INFECTION: DEFINITION OF A NEW SUBGROUP OF PATIENTS ELIGIBLE FOR ANTIVIRAL TREATMENT

2003 ◽  
Vol 98 ◽  
pp. S90-S91
Author(s):  
Guilherme Macedo ◽  
Susana Lopes ◽  
Fernando Araujo ◽  
Fatima Carneiro ◽  
Tavarela Veloso
Keyword(s):  
Hepatitis B Virus ◽  
Virus Infection ◽  
Hepatitis B ◽  
Antiviral Treatment ◽  
Hepatitis B Virus Infection ◽  
B Virus ◽  
Definition Of

scholarly journals Isolation of peptides from phage-displayed random peptide libraries that interact with the talin-binding domain of vinculin

1997 ◽  
Vol 324 (2) ◽  
pp. 523-528 ◽  
Author(s):  
Nils. B ADEY ◽  
Brian. K KAY
Keyword(s):  
Amino Acid ◽  
Sequence Similarity ◽  
Combinatorial Libraries ◽  
Binding Domain ◽  
Peptide Libraries ◽  
Biologically Relevant ◽  
Random Peptide ◽  
Binding Domains ◽  
Random Peptide Libraries ◽  
Binding Peptides

Peptides isolated from combinatorial libraries typically interact with, and thus help to characterize, biologically relevant binding domains of target proteins. To characterize the binding domains of the focal adhesion protein vinculin, vinculin-binding peptides were isolated from two phage-displayed random peptide libraries. Altogether, five non-similar vinculin-binding peptides were identified. Despite the lack of obvious sequence similarity between the peptides, binding and competition studies indicated that all five interact with the talin-binding domain of vinculin and do not disrupt the binding of α-actinin or paxillin to vinculin. The identified peptides and talin bind to vinculin in a comparable manner; both bind to immobilized vinculin, but neither binds to soluble vinculin unless the C-terminus of vinculin has been deleted. An analysis of amino acid variants of one of the peptides has revealed three non-contiguous motifs that also occur in the region of talin previously demonstrated to bind vinculin. Amino acid substitutions within a 127-residue segment of talin capable of binding vinculin confirmed the importance of two of the motifs and suggest that residues critical for binding are within a 16-residue region. This study demonstrates that the vinculin-binding peptides interact with vinculin in a biologically relevant manner and represent an excellent tool for further study of the biochemistry of vinculin.

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