Novel Peptides Based on HIV-1 gp120 Sequence with Homology to Chemokines Inhibit HIV Infection in Cell Culture
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Mendeley | Further Information

{"title"=>"Novel peptides based on HIV-1 gp120 sequence with homology to chemokines inhibit HIV infection in cell culture", "type"=>"journal", "authors"=>[{"first_name"=>"Oleg", "last_name"=>"Chertov", "scopus_author_id"=>"7004585295"}, {"first_name"=>"Ning", "last_name"=>"Zhang", "scopus_author_id"=>"7401648579"}, {"first_name"=>"Xin", "last_name"=>"Chen", "scopus_author_id"=>"15031596300"}, {"first_name"=>"Joost J.", "last_name"=>"Oppenheim", "scopus_author_id"=>"35404740800"}, {"first_name"=>"Jacek", "last_name"=>"Lubkowski", "scopus_author_id"=>"7004334420"}, {"first_name"=>"Connor", "last_name"=>"McGrath", "scopus_author_id"=>"7102335544"}, {"first_name"=>"Raymond C.", "last_name"=>"Sowder", "scopus_author_id"=>"35428095200"}, {"first_name"=>"Bruce J.", "last_name"=>"Crise", "scopus_author_id"=>"6601991665"}, {"first_name"=>"Anatoli", "last_name"=>"Malyguine", "scopus_author_id"=>"6701862923"}, {"first_name"=>"Michele A.", "last_name"=>"Kutzler", "scopus_author_id"=>"6602480444"}, {"first_name"=>"Amber D.", "last_name"=>"Steele", "scopus_author_id"=>"7102182926"}, {"first_name"=>"Earl E.", "last_name"=>"Henderson", "scopus_author_id"=>"35556217200"}, {"first_name"=>"Thomas J.", "last_name"=>"Rogers", "scopus_author_id"=>"7202089170"}], "year"=>2011, "source"=>"PLoS ONE", "identifiers"=>{"scopus"=>"2-s2.0-79251587133", "pmid"=>"21264298", "sgr"=>"79251587133", "doi"=>"10.1371/journal.pone.0014474", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "issn"=>"19326203", "pui"=>"361180200"}, "id"=>"a0b82018-de98-3b57-a07d-0c82f889f8c4", "abstract"=>"The sequential interaction of the envelope glycoprotein of the human immunodeficiency virus type 1 (HIV-1) with CD4 and certain chemokine coreceptors initiates host cell entry of the virus. The appropriate chemokines have been shown to inhibit viral replication by blocking interaction of the gp120 envelope protein with the coreceptors. We considered the possibility that this interaction involves a motif of the gp120 that may be structurally homologous to the chemokines. In the amino acid sequences of most chemokines there is a Trp residue located at the beginning of the C-terminal α-helix, which is separated by six residues from the fourth Cys residue. The gp120 of all HIV-1 isolates have a similar motif, which includes the C-terminal part of a variable loop 3 (V3) and N-terminal part of a conserved region 3 (C3). Two synthetic peptides, derived from the relevant gp120 sequence inhibited HIV-1 replication in macrophages and T lymphocytes in sequence-dependent manner. The peptides also prevented binding of anti-CXCR4 antibodies to CXCR4, and inhibited the intracellular Ca(2+) influx in response to CXCL12/SDF-1α. Thus these peptides can be used to dissect gp120 interactions with chemokine receptors and could serve as leads for the design of new inhibitors of HIV-1.", "link"=>"http://www.mendeley.com/research/novel-peptides-based-hiv1-gp120-sequence-homology-chemokines-inhibit-hiv-infection-cell-culture", "reader_count"=>23, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>1, "Student > Doctoral Student"=>2, "Researcher"=>5, "Student > Ph. D. Student"=>2, "Student > Postgraduate"=>4, "Student > Master"=>2, "Other"=>2, "Student > Bachelor"=>3}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>1, "Student > Doctoral Student"=>2, "Researcher"=>5, "Student > Ph. D. Student"=>2, "Student > Postgraduate"=>4, "Student > Master"=>2, "Other"=>2, "Student > Bachelor"=>3}, "reader_count_by_subject_area"=>{"Unspecified"=>4, "Biochemistry, Genetics and Molecular Biology"=>2, "Agricultural and Biological Sciences"=>10, "Medicine and Dentistry"=>6, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>6}, "Chemistry"=>{"Chemistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>10}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}, "Unspecified"=>{"Unspecified"=>4}}, "reader_count_by_country"=>{"Brazil"=>1}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/807054"], "description"=>"<p>Cells were treated with 15K and 15D, at the designated concentrations, and supernatants were collected from the cultures at 48 h, and subjected to ELISA for the determination of CCL2, CCL3, CCL4, CCL5 and CXCL12 levels. Levels of chemokine at 24, 72, and 96 h were also monitored for chemokine levels (data not shown). Data are presented as the mean (± SD) of triplicate determinations, and the data are representative of the results from experiments with three donors.</p>", "links"=>[], "tags"=>["chemokine", "peptide"], "article_id"=>477414, "categories"=>["Immunology", "Medicine"], "users"=>["Oleg Chertov", "Ning Zhang", "Xin Chen", "Joost J. Oppenheim", "Jacek Lubkowski", "Connor McGrath", "Raymond C. Sowder II", "Bruce J. Crise", "Anatoli Malyguine", "Michele A. Kutzler", "Amber D. Steele", "Earl E. Henderson", "Thomas J. Rogers"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014474.g006", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Induction_of_chemokine_expression_following_peptide_administration_/477414", "title"=>"Induction of chemokine expression following peptide administration.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 21:21:00"}
  • {"files"=>["https://ndownloader.figshare.com/files/806644"], "description"=>"<p>Cells were treated with the designated concentrations of peptide for a period of 1 h prior to addition of HIV-1 at an MOI of 0.1, or 500 nM peptide in Panels E&F. Four h after infection the cells were harvested and the HIV early replication was determined by PCR quantification of either strong-stop proviral R/U5 long-terminal repeat structures (Panels A& B), or at 18 hrs for the measurement of the 5′LTR (Panels C&D). The expression of HIV-1 p24 was also determined as a measure of HIV replication (Panels E&F). Results are presented for a representative experiment except for the data in Panels C and D where the collective data for all experiments are presented as the mean ± SD for each data point.</p>", "links"=>[], "tags"=>["hiv-1", "peptides", "scrambled", "peptide", "15ks", "jrfl", "purified", "monocytes", "pbmcs", "iiib", "cd4-positive", "cells"], "article_id"=>476966, "categories"=>["Immunology", "Medicine"], "users"=>["Oleg Chertov", "Ning Zhang", "Xin Chen", "Joost J. Oppenheim", "Jacek Lubkowski", "Connor McGrath", "Raymond C. Sowder II", "Bruce J. Crise", "Anatoli Malyguine", "Michele A. Kutzler", "Amber D. Steele", "Earl E. Henderson", "Thomas J. Rogers"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014474.g001", "stats"=>{"downloads"=>1, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Inhibition_of_HIV_1_infection_by_peptides_15K_15D_and_the_scrambled_peptide_15KS_using_HIV_1_strain_JRFL_infection_of_purified_monocytes_Panel_A_or_PBMCs_Panels_C_amp_E_or_HIV_1_strain_IIIB_infection_of_purified_CD4_positive_T_cells_Panel_B_or_PBMCs_Pane/476966", "title"=>"Inhibition of HIV-1 infection by peptides 15K, 15D, and the scrambled peptide 15KS using HIV-1 strain JRFL infection of purified monocytes (Panel A) or PBMCs (Panels C&E), or HIV-1 strain IIIB infection of purified CD4-positive T cells (Panel B) or PBMCs (Panel D&F).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 21:18:32"}
  • {"files"=>["https://ndownloader.figshare.com/files/807285"], "description"=>"<p>Sequences of synthesized peptides.</p>", "links"=>[], "tags"=>["synthesized"], "article_id"=>477642, "categories"=>["Immunology", "Medicine"], "users"=>["Oleg Chertov", "Ning Zhang", "Xin Chen", "Joost J. Oppenheim", "Jacek Lubkowski", "Connor McGrath", "Raymond C. Sowder II", "Bruce J. Crise", "Anatoli Malyguine", "Michele A. Kutzler", "Amber D. Steele", "Earl E. Henderson", "Thomas J. Rogers"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014474.t002", "stats"=>{"downloads"=>8, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Sequences_of_synthesized_peptides_/477642", "title"=>"Sequences of synthesized peptides.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 21:22:15"}
  • {"files"=>["https://ndownloader.figshare.com/files/806878"], "description"=>"<p>Cells loaded with Fura-2 were preincubated with peptides at a final concentration of 1.8 mM for 12 sec prior to stimulation with CXCL12 (15 nM).</p>", "links"=>[], "tags"=>["peptides", "15k", "15ks", "pre-treatment", "mobilization", "intracellular", "cells"], "article_id"=>477228, "categories"=>["Immunology", "Medicine"], "users"=>["Oleg Chertov", "Ning Zhang", "Xin Chen", "Joost J. Oppenheim", "Jacek Lubkowski", "Connor McGrath", "Raymond C. Sowder II", "Bruce J. Crise", "Anatoli Malyguine", "Michele A. Kutzler", "Amber D. Steele", "Earl E. Henderson", "Thomas J. Rogers"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014474.g004", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effect_of_peptides_15K_and_15KS_pre_treatment_on_the_mobilization_of_intracellular_Ca_2_in_CXCR4_HEK_cells_in_response_to_CXCL12_/477228", "title"=>"Effect of peptides 15K and 15KS pre-treatment on the mobilization of intracellular Ca<sup>2+</sup> in CXCR4/HEK cells in response to CXCL12.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 21:19:59"}
  • {"files"=>["https://ndownloader.figshare.com/files/806717"], "description"=>"<p>Monocyte-derived macrophages were treated with the designated concentrations of peptide for a period of 1 h prior to addition of HIV-1<sub>JRFL</sub>. After 2 hr, cells were washed, and viral replication was determined after 72 hr by p24 analysis. Results are representative of 4 independent experiments. The level of replication in the 15D and 15K groups were significantly different (P<0.01) from the untreated group at concentrations of 5 nM or more.</p>", "links"=>[], "tags"=>["hiv-1", "jrfl", "monocyte-derived", "macrophages", "peptides", "15d", "chemokine"], "article_id"=>477070, "categories"=>["Immunology", "Medicine"], "users"=>["Oleg Chertov", "Ning Zhang", "Xin Chen", "Joost J. Oppenheim", "Jacek Lubkowski", "Connor McGrath", "Raymond C. Sowder II", "Bruce J. Crise", "Anatoli Malyguine", "Michele A. Kutzler", "Amber D. Steele", "Earl E. Henderson", "Thomas J. Rogers"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014474.g002", "stats"=>{"downloads"=>1, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Inhibition_of_HIV_1_strain_JRFL_infection_of_monocyte_derived_macrophages_by_peptides_15K_15D_and_chemokine_CCL4_/477070", "title"=>"Inhibition of HIV-1 strain JRFL infection of monocyte-derived macrophages by peptides 15K, 15D and chemokine CCL4.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 21:19:06"}
  • {"files"=>["https://ndownloader.figshare.com/files/806796"], "description"=>"<p>A. Dose-dependent effect of peptide 15K in comparison with CXCL12. B. The comparison of the effects of 15K and 15D. C. The comparison of the effects of 15K and 15KS. Cells were preincubated at 22°C with peptides at designated concentrations or CXCL12 for 60 min. Then cells were incubated with FITC-labeled anti-human CXCR4 monoclonal antibodies 12G5 for 40 min at 22°C and washed with FACS buffer prior to flow cytometry.</p>", "links"=>[], "tags"=>["peptides", "15d", "scrambled", "peptide", "15ks", "binding", "anti-cxcr4", "antibody", "12g5", "cemx174"], "article_id"=>477135, "categories"=>["Immunology", "Medicine"], "users"=>["Oleg Chertov", "Ning Zhang", "Xin Chen", "Joost J. Oppenheim", "Jacek Lubkowski", "Connor McGrath", "Raymond C. Sowder II", "Bruce J. Crise", "Anatoli Malyguine", "Michele A. Kutzler", "Amber D. Steele", "Earl E. Henderson", "Thomas J. Rogers"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014474.g003", "stats"=>{"downloads"=>1, "page_views"=>17, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effect_of_peptides_15K_15D_and_scrambled_peptide_15KS_on_the_binding_of_anti_CXCR4_antibody_12G5_to_CEMx174_cells_/477135", "title"=>"Effect of peptides 15K, 15D and scrambled peptide 15KS on the binding of anti-CXCR4 antibody 12G5 to CEMx174 cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 21:19:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/807144"], "description"=>"<p>Gp120 is shown in green and CCL4 is in purple. The solvent interface in the context of both of the whole proteins is to the right of the figure. The gp120 fragment was rotated and side chain residues were allowed to move within the constraints of the CVFF mechanics employed (see <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0014474#s2\" target=\"_blank\">Methods</a>: Computer modeling) in order to align homologous amino acids. Both structures exhibit a buried Trp residue at a turn preceding an α-helix which has polar side chains on the surface. The location of the Trp in the start of the helix and the hydrophobic nature of the residues surrounding the Trp are also conserved features in both structures.</p>", "links"=>[], "tags"=>["structures", "fragments", "gp120", "residues", "pdb", "ccl4"], "article_id"=>477498, "categories"=>["Immunology", "Medicine"], "users"=>["Oleg Chertov", "Ning Zhang", "Xin Chen", "Joost J. Oppenheim", "Jacek Lubkowski", "Connor McGrath", "Raymond C. Sowder II", "Bruce J. Crise", "Anatoli Malyguine", "Michele A. Kutzler", "Amber D. Steele", "Earl E. Henderson", "Thomas J. Rogers"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014474.g007", "stats"=>{"downloads"=>1, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Comparison_of_the_structures_of_the_fragments_of_gp120_HIV_HXB2_residues_331_8211_344_PDB_code_1gc1_and_CCL4_residues_47_8211_64_PDB_code_1hum_/477498", "title"=>"Comparison of the structures of the fragments of gp120 (HIV<sub>HXB2</sub> residues 331–344, PDB code 1gc1) and CCL4 (residues 47–64, PDB code 1hum).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 21:21:23"}
  • {"files"=>["https://ndownloader.figshare.com/files/806983"], "description"=>"<p>(A) Effect of pre-treatment with peptides 15K and 15D on the binding of CCL4 to SupT1/CCR5 cells; (B) Effect of pre-treatment with peptides 15K and 15D on the binding of CXCL12 to CEMx174 cells; and (C) Effect of pre-treatment with 15K and control peptide 15GIG on the binding of CXCL12 to CEMx174 cells; (D) Effect of pre-treatment with peptides 15K and 15KS on the binding of CXCL12 to CEMx174. Binding studies were performed as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0014474#s2\" target=\"_blank\">Materials and Methods</a>.</p>", "links"=>[], "tags"=>["chemokine", "receptor", "ligand", "binding", "peptide"], "article_id"=>477339, "categories"=>["Immunology", "Medicine"], "users"=>["Oleg Chertov", "Ning Zhang", "Xin Chen", "Joost J. Oppenheim", "Jacek Lubkowski", "Connor McGrath", "Raymond C. Sowder II", "Bruce J. Crise", "Anatoli Malyguine", "Michele A. Kutzler", "Amber D. Steele", "Earl E. Henderson", "Thomas J. Rogers"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014474.g005", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Inhibition_of_chemokine_receptor_ligand_binding_by_peptide_pre_treatment_/477339", "title"=>"Inhibition of chemokine receptor ligand binding by peptide pre-treatment.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 21:20:33"}
  • {"files"=>["https://ndownloader.figshare.com/files/807246"], "description"=>"a<p>The residues numbered according to Korber (1998). The residues identical in HIV-1 gp120 and chemokines are shown in bold. The location of the residues relative to the V3 loop/C3 region is noted.</p>", "links"=>[], "tags"=>["alignment", "sequences", "gp120", "hiv-1", "strains", "ccl4"], "article_id"=>477597, "categories"=>["Immunology", "Medicine"], "users"=>["Oleg Chertov", "Ning Zhang", "Xin Chen", "Joost J. Oppenheim", "Jacek Lubkowski", "Connor McGrath", "Raymond C. Sowder II", "Bruce J. Crise", "Anatoli Malyguine", "Michele A. Kutzler", "Amber D. Steele", "Earl E. Henderson", "Thomas J. Rogers"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014474.t001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Amino_acid_alignment_of_sequences_of_gp120_of_some_HIV_1_strains_with_CCL4_and_CXCL12_/477597", "title"=>"Amino acid alignment of sequences of gp120 of some HIV-1 strains with CCL4 and CXCL12.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 21:21:59"}

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