Heavy chain amino acid sequence alignment of V_H4-59 encoded mAbs.

<p>The heavy chain amino acid sequence of HIV-specific V_H4-59 encoded mAbs are shown aligned to the V_H4-59 germline gene. Conservation with the germline gene sequence is indicated by a <b>*</b> symbol in the alignments.</p

Heavy chain gene analysis of Gag-only VLP binding antibodies.

<p>Heavy chain gene analysis of Gag-only VLP binding antibodies.</p

Generation of p17 Matrix deletion mutants.

<p>The full amino acid sequence alignment of the wild-type (WT) Matrix protein and the 10 Matrix deletion mutants. Conserved residues in the Matrix deletion mutants are indicated by the <b>*</b> symbol, and deleted resides indicated by the—symbol.</p

Mapping the mAb 3E4 epitope on the surface of HIV Gag protein.

<p><b>(A)</b> Binding of mAb 3E4 to overlapping linear peptides of the HIV-1 Gag protein. <b>(B)</b> Structural depiction of the mAb 3E4 epitope (shown in red) on the HIV-1 Gag protein. <b>(C)</b> Structural depiction of deletion mutants #1, #3, #4, #5, #6, and #7 (shown in blue, yellow, magenta, cyan, orange or wheat) on the surface of the HIV-1 Gag protein. <b>(D)</b> Western blot analysis of Gag, wild-type Matrix protein, or each of 10 different Matrix protein deletion mutants, using mAb 3E4 as a probe.</p

Binding of V_H4-59 encoded antibodies to HIV antigens.

<p>Binding of mAb b12 or V_H4-59 gene-encoded mAbs at a concentration of 1 μg/mL to Env VLP (black), Gag-only VLP (grey), BaL gp120 (white), or YU2 gp140 (pattern) tested by ELISA.</p

Epitope competition group (CG) assignment, binding kinetics and preference of quaternary-epitope targeting Abs for binding to Env in VLPs gp140 trimers.

<p>Epitope competition group (CG) assignment, binding kinetics and preference of quaternary-epitope targeting Abs for binding to Env in VLPs gp140 trimers.</p

Human Antibodies that Recognize Novel Immunodominant Quaternary Epitopes on the HIV-1 Env Protein

<div><p>Numerous broadly neutralizing antibodies (Abs) target epitopes that are formed or enhanced during mature HIV envelope formation (<i>i</i>.<i>e</i>. quaternary epitopes). Generally, it is thought that Env epitopes that induce broadly neutralizing Abs are difficult to access and poorly immunogenic because of the characteristic oligomerization, conformational flexibility, sequence diversity and extensive glycosylation of Env protein. To enhance for isolation of quaternary epitope-targeting Abs (QtAbs), we previously used HIV virus-like particles (VLPs) to bind B cells from long-term non-progressor subjects to identify a panel of monoclonal Abs. When expressed as recombinant full-length Abs, a subset of these novel Abs exhibited the binding profiles of QtAbs, as they either failed to bind to monomeric Env protein or showed much higher affinity for Env trimers and VLPs. These QtAbs represented a significant proportion of the B-cell response identified with VLPs. The Ab genes of these clones were highly mutated, but they did not neutralize common HIV strains. We sought to further define the epitopes targeted by these QtAbs. Competition-binding and mapping studies revealed these Abs targeted four separate epitopes; they also failed to compete for binding by Abs to known major neutralizing epitopes. Detailed epitope mapping studies revealed that two of the four epitopes were located in the gp41 subunit of Env. These QtAbs bound pre-fusion forms of antigen and showed differential binding kinetics depending on whether oligomers were produced as recombinant gp140 trimers or as full-length Env incorporated into VLPs. Antigenic regions within gp41 present unexpectedly diverse structural epitopes, including these QtAb epitopes, which may be targeted by the naturally occurring Ab response to HIV infection.</p></div

Disruption of mAb binding to HIV-1 gp160 by alanine replacement of amino acid residues.

<p>Disruption of mAb binding to HIV-1 gp160 by alanine replacement of amino acid residues.</p

Quaternary epitope-targeting Abs variably bind gp140 trimers in a strain-dependent manner.

<p>Depending on the QtAb, variability was observed in binding BaL strain Env protein incorporated in VLPs (filled circle) versus gp140 trimers of the same strain (Clade B BaL, filled triangle) or of a different clade B strain (SF162, open triangle). See <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0158861#pone.0158861.t001" target="_blank">Table 1</a> for corresponding binding data.</p

Ferula assa-foetida L.

原著和名: アギ科名: セリ科 = Umbelliferae採集地: 千葉県 千葉市 千葉大学 (下総 千葉市 千葉大学)採集日: 1971/5/23採集者: 萩庭丈壽整理番号: JH037541国立科学博物館整理番号: TNS-VS-987541備考: DB作成協力会による補足あ