Recognition of Membrane-Bound Fusion-Peptide/MPER Complexes by the HIV-1 Neutralizing 2F5 Antibody: Implications for Anti-2F5 Immunogenicity
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{"title"=>"Recognition of Membrane-Bound Fusion-Peptide/MPER Complexes by the HIV-1 Neutralizing 2F5 Antibody: Implications for Anti-2F5 Immunogenicity", "type"=>"journal", "authors"=>[{"first_name"=>"Nerea", "last_name"=>"Huarte", "scopus_author_id"=>"14026762100"}, {"first_name"=>"Aitziber", "last_name"=>"Araujo", "scopus_author_id"=>"55533574000"}, {"first_name"=>"Rocio", "last_name"=>"Arranz", "scopus_author_id"=>"14830939000"}, {"first_name"=>"Maier", "last_name"=>"Lorizate", "scopus_author_id"=>"6507634662"}, {"first_name"=>"Heribert", "last_name"=>"Quendler", "scopus_author_id"=>"9332462900"}, {"first_name"=>"Renate", "last_name"=>"Kunert", "scopus_author_id"=>"6603682350"}, {"first_name"=>"José M.", "last_name"=>"Valpuesta", "scopus_author_id"=>"7004518850"}, {"first_name"=>"José L.", "last_name"=>"Nieva", "scopus_author_id"=>"7004317241"}], "year"=>2012, "source"=>"PLoS ONE", "identifiers"=>{"sgr"=>"84871398941", "pmid"=>"23285173", "pui"=>"366307853", "isbn"=>"1932-6203", "scopus"=>"2-s2.0-84871398941", "doi"=>"10.1371/journal.pone.0052740", "issn"=>"19326203"}, "id"=>"18c3cbc5-0236-3b48-ac6e-2fce73e0783d", "abstract"=>"The membrane proximal external region (MPER) of the fusogenic HIV-1 glycoprotein-41 harbors the epitope sequence recognized by 2F5, a broadly neutralizing antibody isolated from an infected individual. Structural mimicry of the conserved MPER 2F5 epitope constitutes a pursued goal in the field of anti-HIV vaccine development. It has been proposed that 2F5 epitope folding into its native state is attained in the vicinity of the membrane interface and might involve interactions with other viral structures. Here we present results indicating that oligomeric complexes established between MPER and the conserved amino-terminal fusion peptide (FP) can partition into lipid vesicles and be specifically bound by the 2F5 antibody at their surfaces. Cryo-transmission electron microscopy of liposomes doped with MPER:FP peptide mixtures provided the structural grounds for complex recognition by antibody at lipid bilayer surfaces. Supporting the immunogenicity of the membrane-bound complex, these MPER:FP peptide-vesicle formulations could trigger cross-reactive anti-MPER antibodies in rabbits. Thus, our observations suggest that contacts with N-terminal regions of gp41 may stabilize the 2F5 epitope as a membrane-surface antigen.", "link"=>"http://www.mendeley.com/research/recognition-membranebound-fusionpeptidemper-complexes-hiv1-neutralizing-2f5-antibody-implications-an", "reader_count"=>22, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Researcher"=>7, "Student > Ph. D. Student"=>5, "Student > Master"=>1, "Other"=>3, "Student > Bachelor"=>2, "Lecturer"=>1, "Professor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Researcher"=>7, "Student > Ph. D. Student"=>5, "Student > Master"=>1, "Other"=>3, "Student > Bachelor"=>2, "Lecturer"=>1, "Professor"=>2}, "reader_count_by_subject_area"=>{"Engineering"=>1, "Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>3, "Agricultural and Biological Sciences"=>10, "Medicine and Dentistry"=>2, "Business, Management and Accounting"=>1, "Pharmacology, Toxicology and Pharmaceutical Science"=>1, "Chemistry"=>1, "Computer Science"=>1, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Chemistry"=>{"Chemistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>10}, "Computer Science"=>{"Computer Science"=>1}, "Business, Management and Accounting"=>{"Business, Management and Accounting"=>1}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}, "Unspecified"=>{"Unspecified"=>1}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>1}}, "reader_count_by_country"=>{"Portugal"=>1}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/520368"], "description"=>"<p>A) Competitive ELISA assays were performed using plates coated with MPERp/FPp (1.4 µM). Prior to adding to the plates, 10 µg/ml of total (blue) or 0.1 µg/ml of 2F5-specific (red) IgG purified from rabbit sera was pre-incubated for 30 minutes with serial dilutions of 2F5ep competitor and set-up in triplicates. B) Peptide recognition by rabbit IgG purified with 2F5ep-Cys. Antibodies were titrated against 1.4 µM of the following peptides immobilized in ELISA plates: C34 (orange); MPERp (red); CpreTM (green); TMDp (black). Reactivity to 2F5ep is denoted by empty red symbols and dotted line. Specificity of the response for the correct 2F5 epitope was tested using MPERp(9,10)Ala (blue). C) Reactivity with liposome-peptide immunogen by Western blot. Liposome-associated peptides were incubated with 20 µM BS<sup>3+</sup> as described in the caption for Fig. 3A, subsequently resolved by SDS-PAGE electrophoresis, then transferred to a nitrocellulose membrane and finally probed with 2F5ep-specific antibodies. Lanes 1 and 2 display bands corresponding to MPERp/FPp and MPERp(9,10)Ala/FPp mixture samples, respectively. M: molecular weight markers (MW: 17, 10 and 4.6 kDa).</p>", "links"=>[], "tags"=>["2f5", "epitope", "targeting", "antibodies"], "article_id"=>190857, "categories"=>["Virology", "Biochemistry", "Biophysics", "Infectious Diseases", "Immunology"], "users"=>["Nerea Huarte", "Aitziber Araujo", "Rocio Arranz", "Maier Lorizate", "Heribert Quendler", "Renate Kunert", "José M. Valpuesta", "José L. Nieva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0052740.g007", "stats"=>{"downloads"=>1, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Recovery_of_2F5_epitope_targeting_antibodies_from_rabbit_serum_/190857", "title"=>"Recovery of 2F5 epitope targeting antibodies from rabbit serum.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-21 00:14:17"}
  • {"files"=>["https://ndownloader.figshare.com/files/519730"], "description"=>"<p>A) Secondary structures adopted by the <sup>662</sup>ELDKWAS<sup>668</sup> sequence spanning the 2F5 core epitope (depicted in orange), in contact with DPC micelles (left) or in complex with Fab’2F5 (right). Lateral and front views of the structures (PDB accession numbers as indicated in the panel) were rendered using Swiss-PDB-viewer program. B) MPER sequence (top) and membrane topologies proposed for the 2F5 epitope (bottom). Bottom-left: Membrane-inserted MPER peptide. Partitioning from solution constrains 2F5 epitope into a helical structure mostly embedded into the hydrocarbon core (HC) region of the bilayer (red cylinder) <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0052740#pone.0052740-Sun1\" target=\"_blank\">[30]</a>. Bottom-center: Hypothetical MPER structure recognized by MAb2F5 in the vicinity of the membrane interface (MI). (1) and (2) respectively indicate the structure bound to the high-affinity binding site and the surface putatively contacted by the hydrophobic loop <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0052740#pone.0052740-Julien2\" target=\"_blank\">[38]</a>, <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0052740#pone.0052740-Guenaga1\" target=\"_blank\">[39]</a>. Bottom-right: Proposed FP effect on 2F5 epitope stabilization. FP residues (blue arrow) may retain the 2F5 epitope β-turn structure at membrane interfaces <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0052740#pone.0052740-Julien1\" target=\"_blank\">[27]</a> and orient downstream residues for additional antibody docking. The 2F5 epitope region has been depicted as in the structure with PDB entry 3D0L (asterisk). Green side-chains designate hydrophobic residues.</p>", "links"=>[], "tags"=>["2f5", "epitope", "membrane"], "article_id"=>190215, "categories"=>["Virology", "Biochemistry", "Biophysics", "Infectious Diseases", "Immunology"], "users"=>["Nerea Huarte", "Aitziber Araujo", "Rocio Arranz", "Maier Lorizate", "Heribert Quendler", "Renate Kunert", "José M. Valpuesta", "José L. Nieva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0052740.g001", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Proposed_organization_for_the_2F5_epitope_at_membrane_interfaces_/190215", "title"=>"Proposed organization for the 2F5 epitope at membrane interfaces.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-21 00:03:35"}
  • {"files"=>["https://ndownloader.figshare.com/files/520442"], "description"=>"a<p>sequences and numbering are derived from the prototypic HXBc2 isolate.</p>", "links"=>[], "tags"=>["sequences", "2f5", "epitope", "residues"], "article_id"=>190929, "categories"=>["Virology", "Biochemistry", "Biophysics", "Infectious Diseases", "Immunology"], "users"=>["Nerea Huarte", "Aitziber Araujo", "Rocio Arranz", "Maier Lorizate", "Heribert Quendler", "Renate Kunert", "José M. Valpuesta", "José L. Nieva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0052740.t001", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Peptide_sequences_used_in_this_study_core_2F5_epitope_residues_underlined_/190929", "title"=>"Peptide sequences used in this study (core 2F5 epitope residues underlined).", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2012-12-21 00:15:29"}
  • {"files"=>["https://ndownloader.figshare.com/files/519927"], "description"=>"<p>A) Western blot analyses of MPER-based peptides pre-incubated with lipid vesicles at a peptide-to-lipid ratio of 1∶50, prior to cross-linking with 20 µM BS<sup>3+</sup> and electrophoresis. Conditions otherwise as in previous Fig. 2A. B) Evaluation of complex-membrane association by vesicle floatation. Peptide-containing vesicles (added peptide-to-lipid ratio of 1∶50) were treated with 20 µM BS<sup>3+</sup> cross-linker and then subjected to ultracentrifugation (627,000×g) 120 min in D<sub>2</sub>O buffer. Left panel: Fluorescence emission of Rhodamine-labeled POPC:Chol (2∶1) LUV recovered from floating (red-solid) and non-floating (black-dotted) fractions. Center Panel: MPERp and FPp co-floating with vesicles were detected by Western blotting with MAb2F5 or following NBD fluorescence, respectively. Right panel: Percentage of peptide in floating and non-floating fractions (red and black bars, respectively) in the presence and absence of vesicles (LUVs).</p>", "links"=>[], "tags"=>["complexes"], "article_id"=>190414, "categories"=>["Virology", "Biochemistry", "Biophysics", "Infectious Diseases", "Immunology"], "users"=>["Nerea Huarte", "Aitziber Araujo", "Rocio Arranz", "Maier Lorizate", "Heribert Quendler", "Renate Kunert", "José M. Valpuesta", "José L. Nieva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0052740.g003", "stats"=>{"downloads"=>3, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Preservation_of_MPER_FP_complexes_upon_association_with_membranes_/190414", "title"=>"Preservation of MPER/FP complexes upon association with membranes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-21 00:06:54"}
  • {"files"=>["https://ndownloader.figshare.com/files/520020"], "description"=>"<p>A) The MAb2F5 was incubated with a stirred solution of f-DHPE-labeled LUV (250 µM). After 10 minutes, the fluorescently labeled secondary Ab was added and the resulting mixtures were incubated for 5 minutes before being analyzed by flow cytometry. Top panels: the samples in the absence of MAb show a single particle population that corresponds to DHPE-labeled vesicles. Bottom panels: the incubation with 15 µg/ml of MAb rendered double labeled vesicles in MPERp:FPp mixture-containing samples (center), but not in MPERp- (left) or FPp (right) containing samples. This pattern could not be observed in the absence of the MAbs (top panels). B) Specificity of FPp effect on MAb2F5-vesicle association as detected by FACS. MAb2F5 was incubated at the final concentrations indicated in the panels with MPERp:FPp mixture-, MPERp- or MPERp:FPctl mixture-containing LUV (red, blue and green traces, respectively) under conditions that were otherwise similar to those in the previous panel.</p>", "links"=>[], "tags"=>["immunology", "Virology", "Infectious diseases", "biophysics", "Biochemistry"], "article_id"=>190507, "categories"=>["Virology", "Biochemistry", "Biophysics", "Infectious Diseases", "Immunology"], "users"=>["Nerea Huarte", "Aitziber Araujo", "Rocio Arranz", "Maier Lorizate", "Heribert Quendler", "Renate Kunert", "José M. Valpuesta", "José L. Nieva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0052740.g004", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MAb_vesicle_association_as_determined_by_flow_cytometry_/190507", "title"=>"MAb-vesicle association as determined by flow cytometry.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-21 00:08:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/280785", "https://ndownloader.figshare.com/files/280831", "https://ndownloader.figshare.com/files/280860", "https://ndownloader.figshare.com/files/281077", "https://ndownloader.figshare.com/files/281142", "https://ndownloader.figshare.com/files/281219"], "description"=>"<div><p>The membrane proximal external region (MPER) of the fusogenic HIV-1 glycoprotein-41 harbors the epitope sequence recognized by 2F5, a broadly neutralizing antibody isolated from an infected individual. Structural mimicry of the conserved MPER 2F5 epitope constitutes a pursued goal in the field of anti-HIV vaccine development. It has been proposed that 2F5 epitope folding into its native state is attained in the vicinity of the membrane interface and might involve interactions with other viral structures. Here we present results indicating that oligomeric complexes established between MPER and the conserved amino-terminal fusion peptide (FP) can partition into lipid vesicles and be specifically bound by the 2F5 antibody at their surfaces. Cryo-transmission electron microscopy of liposomes doped with MPER:FP peptide mixtures provided the structural grounds for complex recognition by antibody at lipid bilayer surfaces. Supporting the immunogenicity of the membrane-bound complex, these MPER:FP peptide-vesicle formulations could trigger cross-reactive anti-MPER antibodies in rabbits. Thus, our observations suggest that contacts with N-terminal regions of gp41 may stabilize the 2F5 epitope as a membrane-surface antigen.</p> </div>", "links"=>[], "tags"=>["membrane-bound", "complexes", "hiv-1", "neutralizing", "2f5", "implications", "anti-2f5", "immunogenicity"], "article_id"=>115365, "categories"=>["Cancer", "Biochemistry", "Biophysics", "Immunology"], "users"=>["Nerea Huarte", "Aitziber Araujo", "Rocio Arranz", "Maier Lorizate", "Heribert Quendler", "Renate Kunert", "José M. Valpuesta", "José L. Nieva"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0052740.s001", "https://dx.doi.org/10.1371/journal.pone.0052740.s002", "https://dx.doi.org/10.1371/journal.pone.0052740.s003", "https://dx.doi.org/10.1371/journal.pone.0052740.s004", "https://dx.doi.org/10.1371/journal.pone.0052740.s005", "https://dx.doi.org/10.1371/journal.pone.0052740.s006"], "stats"=>{"downloads"=>10, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Recognition_of_Membrane_Bound_Fusion_Peptide_MPER_Complexes_by_the_HIV_1_Neutralizing_2F5_Antibody_Implications_for_Anti_2F5_Immunogenicity__/115365", "title"=>"Recognition of Membrane-Bound Fusion-Peptide/MPER Complexes by the HIV-1 Neutralizing 2F5 Antibody: Implications for Anti-2F5 Immunogenicity", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-12-21 01:29:25"}
  • {"files"=>["https://ndownloader.figshare.com/files/519814"], "description"=>"<p>A) Peptides (10 µg) were processed by SDS-PAGE, and subsequently detected by Western blotting using 2F5 antibody. In some instances, peptides were pre-incubated with cross-linker (20 µM BS<sup>3+</sup>). Samples were loaded onto the gel as follows: (1) MPERp; (2) MPERp/BS<sup>3+</sup>; (3) MPERp(9,10)Ala/BS<sup>3+</sup>; (4) MPERp:FPp (1∶1) mixture; (5) MPERp:FPp/BS<sup>3+</sup>; (6) MPERp(9,10)Ala:FPp/BS<sup>3+</sup>; (7) MPERp:FPctl/BS<sup>3+</sup>; (8) FPp/BS<sup>3+</sup>; (9) FPctl/BS<sup>3+</sup>. M: positions of the molecular weight markers (MW: 17, 10 and 4.6 kDa). B) Fluorescence detection of NBD-labeled FPp in SDS-PAGE gels. All samples were incubated with 20 µM BS<sup>3+</sup> before electrophoresis. The migration of molecular weight standard proteins is indicated in the frame.</p>", "links"=>[], "tags"=>["analyses"], "article_id"=>190308, "categories"=>["Virology", "Biochemistry", "Biophysics", "Infectious Diseases", "Immunology"], "users"=>["Nerea Huarte", "Aitziber Araujo", "Rocio Arranz", "Maier Lorizate", "Heribert Quendler", "Renate Kunert", "José M. Valpuesta", "José L. Nieva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0052740.g002", "stats"=>{"downloads"=>1, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Electrophoretic_analyses_of_MPERp_FPp_complex_formation_/190308", "title"=>"Electrophoretic analyses of MPERp/FPp complex formation.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-21 00:05:08"}
  • {"files"=>["https://ndownloader.figshare.com/files/520127"], "description"=>"<p>A) MAb2F5 capacity for inhibiting gp41-mediated cell-cell fusion. B) Pre-incubation with LUVs containing the MPERp:FPp mixture (red circles), the MPERp only (blue squares), or the MPERp:FPctl mixture (green triangles) restores gp41-mediated cell-cell fusion that is otherwise inhibited by MAb2F5. MAb was applied at 5 µg/well in these assays. Lipid and membrane-bound peptide concentrations were 500 and 4.5 µM, respectively. Significant differences are indicated (**p<0.005; *p<0.05). Means ± SD of four experimental determinations are displayed in both panels.</p>", "links"=>[], "tags"=>["mab2f5-mediated", "fusion", "inhibition", "pre-incubation", "peptide", "complexes"], "article_id"=>190610, "categories"=>["Virology", "Biochemistry", "Biophysics", "Infectious Diseases", "Immunology"], "users"=>["Nerea Huarte", "Aitziber Araujo", "Rocio Arranz", "Maier Lorizate", "Heribert Quendler", "Renate Kunert", "José M. Valpuesta", "José L. Nieva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0052740.g005", "stats"=>{"downloads"=>0, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Reversion_of_MAb2F5_mediated_fusion_inhibition_after_pre_incubation_with_MPERp_FPp_peptide_complexes_on_LUV_/190610", "title"=>"Reversion of MAb2F5-mediated fusion inhibition after pre-incubation with MPERp/FPp peptide complexes on LUV.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-21 00:10:10"}
  • {"files"=>["https://ndownloader.figshare.com/files/520259"], "description"=>"<p>Micrographs correspond to LUV pre-incubated with MPERp:FPp mixture (complex-to-lipid mole ratio of 1∶100), that were subsequently incubated for 20 seconds with MAb2F5 (paratope-to-peptide ratio of 1∶10) before vitrification (left panel), or vitrified after 5 minutes of incubation with double concentration of MAb (paratope-to-peptide ratio, 1∶5) (right panel). Arrows point to rods of approximately 10–12 nm that protrude from the bilayer surface, while asterisks indicate electrodense particles. Both vesicles are shown at the same magnification. Cartoons on top depict the interpretation for the observed structures (see text). In the right micrograph, gold particle’s diameter was 10 nm (bottom right corner).</p>", "links"=>[], "tags"=>["membrane-bound"], "article_id"=>190751, "categories"=>["Virology", "Biochemistry", "Biophysics", "Infectious Diseases", "Immunology"], "users"=>["Nerea Huarte", "Aitziber Araujo", "Rocio Arranz", "Maier Lorizate", "Heribert Quendler", "Renate Kunert", "José M. Valpuesta", "José L. Nieva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0052740.g006", "stats"=>{"downloads"=>3, "page_views"=>17, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MAb2F5_recognition_of_membrane_bound_MPERp_FPp_complex_by_cryo_TEM_/190751", "title"=>"MAb2F5 recognition of membrane-bound MPERp/FPp complex by cryo-TEM.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-21 00:12:31"}

PMC Usage Stats | Further Information

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Relative Metric

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