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HbAHP-25, an In-Silico Designed Peptide, Inhibits HIV-1 Entry by Blocking gp120 Binding to CD4 Receptor.

Human Immunodeficiency Virus (HIV-1) poses a serious threat to the developing world and sexual transmission continues to be the major source of new infections. Therefore, the development of molecules, which prevent new HIV-1 infections, is highly warranted. In the present study, a panel of human hem... Full description

Journal Title: PloS one 2015, Vol.10(4), p.e0124839
Main Author: Bashir, Tahir
Other Authors: Patgaonkar, Mandar , Kumar, Selvaa C , Pasi, Achhelal , Reddy, Kudumula Venkata Rami
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0124839
Link: http://search.proquest.com/docview/1677886780/?pq-origsite=primo
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recordid: proquest1677886780
title: HbAHP-25, an In-Silico Designed Peptide, Inhibits HIV-1 Entry by Blocking gp120 Binding to CD4 Receptor.
format: Article
creator:
  • Bashir, Tahir
  • Patgaonkar, Mandar
  • Kumar, Selvaa C
  • Pasi, Achhelal
  • Reddy, Kudumula Venkata Rami
subjects:
  • Adult–Chemistry
  • Amino Acid Sequence–Immunology
  • Animals–Metabolism
  • Antibodies, Monoclonal–Drug Effects
  • Cd4 Antigens–Immunology
  • Cell Line–Immunology
  • Cell Survival–Metabolism
  • Epitopes–Chemistry
  • Female–Metabolism
  • HIV Antibodies–Chemistry
  • HIV Core Protein P24–Pharmacology
  • HIV Envelope Protein Gp120–Drug Therapy
  • HIV Fusion Inhibitors–Virology
  • HIV Infections–Drug Effects
  • HIV-1–Physiology
  • Hemoglobins–Chemistry
  • Humans–Pharmacology
  • Male–Chemistry
  • Models, Molecular–Chemistry
  • Molecular Sequence Data–Pharmacology
  • Peptide Fragments–Drug Effects
  • Peptides–Drug Effects
  • Protein Binding–Drug Effects
  • Protein Conformation–Drug Effects
  • Protein Interaction Domains and Motifs–Drug Effects
  • Rats–Drug Effects
  • Virus Internalization–Drug Effects
  • Young Adult–Drug Effects
  • Antibodies, Monoclonal
  • Cd4 Antigens
  • Epitopes
  • HIV Antibodies
  • HIV Core Protein P24
  • HIV Envelope Protein Gp120
  • HIV Fusion Inhibitors
  • Hbahp-25
  • Hemoglobins
  • Peptide Fragments
  • Peptides
  • Alpha(A) Globin
ispartof: PloS one, 2015, Vol.10(4), p.e0124839
description: Human Immunodeficiency Virus (HIV-1) poses a serious threat to the developing world and sexual transmission continues to be the major source of new infections. Therefore, the development of molecules, which prevent new HIV-1 infections, is highly warranted. In the present study, a panel of human hemoglobin (Hb)-[alpha] subunit derived peptides and their analogues, with an ability to bind gp120, were designed in-silico and their anti-HIV-1 activity was evaluated. Of these peptides, HbAHP-25, an analogue of Hb-[alpha] derived peptide, demonstrated significant anti-HIV-1 activity. HbAHP-25 was found to be active against CCR5-tropic HIV-1 strains (ADA5 and BaL) and CXCR4-tropic HIV-1 strains (IIIB and NL4-3). Surface plasmon resonance (SPR) and ELISA revealed direct interaction between HbAHP-25 and HIV-1 envelope protein, gp120. The peptide prevented binding of CD4 to gp120 and blocked subsequent steps leading to entry and/or fusion or both. Anti-HIV activity of HbAHP-25 appeared to be specific as it failed to inhibit the entry of HIV-1 pseudotyped virus (HIV-1 VSV). Further, HbAHP-25 was found to be non-cytotoxic to TZM-bl cells, VK2/E6E7 cells, CEM-GFP cells and PBMCs, even at higher concentrations. Moreover, HbAHP-25 retained its anti-HIV activity in presence of seminal plasma and vaginal fluid. In brief, the study identified HbAHP-25, a novel anti-HIV peptide, which directly interacts with gp120 and thus has a potential to inhibit early stages of HIV-1 infection.
language: eng
source:
identifier: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0124839
fulltext: fulltext
issn:
  • 19326203
  • 1932-6203
url: Link


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titleHbAHP-25, an In-Silico Designed Peptide, Inhibits HIV-1 Entry by Blocking gp120 Binding to CD4 Receptor.
creatorBashir, Tahir ; Patgaonkar, Mandar ; Kumar, Selvaa C ; Pasi, Achhelal ; Reddy, Kudumula Venkata Rami
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identifierE-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0124839
subjectAdult–Chemistry ; Amino Acid Sequence–Immunology ; Animals–Metabolism ; Antibodies, Monoclonal–Drug Effects ; Cd4 Antigens–Immunology ; Cell Line–Immunology ; Cell Survival–Metabolism ; Epitopes–Chemistry ; Female–Metabolism ; HIV Antibodies–Chemistry ; HIV Core Protein P24–Pharmacology ; HIV Envelope Protein Gp120–Drug Therapy ; HIV Fusion Inhibitors–Virology ; HIV Infections–Drug Effects ; HIV-1–Physiology ; Hemoglobins–Chemistry ; Humans–Pharmacology ; Male–Chemistry ; Models, Molecular–Chemistry ; Molecular Sequence Data–Pharmacology ; Peptide Fragments–Drug Effects ; Peptides–Drug Effects ; Protein Binding–Drug Effects ; Protein Conformation–Drug Effects ; Protein Interaction Domains and Motifs–Drug Effects ; Rats–Drug Effects ; Virus Internalization–Drug Effects ; Young Adult–Drug Effects ; Antibodies, Monoclonal ; Cd4 Antigens ; Epitopes ; HIV Antibodies ; HIV Core Protein P24 ; HIV Envelope Protein Gp120 ; HIV Fusion Inhibitors ; Hbahp-25 ; Hemoglobins ; Peptide Fragments ; Peptides ; Alpha(A) Globin
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descriptionHuman Immunodeficiency Virus (HIV-1) poses a serious threat to the developing world and sexual transmission continues to be the major source of new infections. Therefore, the development of molecules, which prevent new HIV-1 infections, is highly warranted. In the present study, a panel of human hemoglobin (Hb)-[alpha] subunit derived peptides and their analogues, with an ability to bind gp120, were designed in-silico and their anti-HIV-1 activity was evaluated. Of these peptides, HbAHP-25, an analogue of Hb-[alpha] derived peptide, demonstrated significant anti-HIV-1 activity. HbAHP-25 was found to be active against CCR5-tropic HIV-1 strains (ADA5 and BaL) and CXCR4-tropic HIV-1 strains (IIIB and NL4-3). Surface plasmon resonance (SPR) and ELISA revealed direct interaction between HbAHP-25 and HIV-1 envelope protein, gp120. The peptide prevented binding of CD4 to gp120 and blocked subsequent steps leading to entry and/or fusion or both. Anti-HIV activity of HbAHP-25 appeared to be specific as it failed to inhibit the entry of HIV-1 pseudotyped virus (HIV-1 VSV). Further, HbAHP-25 was found to be non-cytotoxic to TZM-bl cells, VK2/E6E7 cells, CEM-GFP cells and PBMCs, even at higher concentrations. Moreover, HbAHP-25 retained its anti-HIV activity in presence of seminal plasma and vaginal fluid. In brief, the study identified HbAHP-25, a novel anti-HIV peptide, which directly interacts with gp120 and thus has a potential to inhibit early stages of HIV-1 infection.
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titleHbAHP-25, an In-Silico Designed Peptide, Inhibits HIV-1 Entry by Blocking gp120 Binding to CD4 Receptor.
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