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. 1998 Jan 5;187(1):25–35. doi: 10.1084/jem.187.1.25

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(A) Map showing the position of snythetic gp120 peptides with respect to gp120 C2-V3-C3 domains and TSP-binding motifs. A set of gp120mn peptides (∼20 aa) were immobilized either singly (numbered 1–7) or in pairs as indicated. Corresponding amino acid positions are: 1, aa 271–290; 2, aa 281–300; 3, aa 291–310; 4, aa 311–330; 5, aa 331–351; 6, aa 351–370; 7, aa 3361–380; 1+2 and 6+7 overlap by 10 aa; gp120, full length rgp120mn; V3 loop, aa 305–332; motif 1, aa 272–321; motif 2, aa 331–384. (B) Binding of ¹²⁵I-TSP1 to gp120 peptides. Increasing concentrations of soluble ¹²⁵I-labeled TSP1 (25 nM–1 μM) were added to immobilized gp120mn peptides. Samples were incubated and bound TSP1 was measured as in Fig. 2. Shown is a single data set for 25 nM TSP1 binding to ∼75–130 μmol peptide or ∼2 μmol gp120.

(A) Map showing the position of snythetic gp120 peptides with respect to gp120 C2-V3-C3 domains and TSP-binding motifs. A set of gp120mn peptides (∼20 aa) were immobilized either singly (numbered 1–7) or in pairs as indicated. Corresponding amino acid positions are: 1, aa 271–290; 2, aa 281–300; 3, aa 291–310; 4, aa 311–330; 5, aa 331–351; 6, aa 351–370; 7, aa 3361–380; 1+2 and 6+7 overlap by 10 aa; gp120, full length rgp120mn; V3 loop, aa 305–332; motif 1, aa 272–321; motif 2, aa 331–384. (B) Binding of ¹²⁵I-TSP1 to gp120 peptides. Increasing concentrations of soluble ¹²⁵I-labeled TSP1 (25 nM–1 μM) were added to immobilized gp120mn peptides. Samples were incubated and bound TSP1 was measured as in Fig. 2. Shown is a single data set for 25 nM TSP1 binding to ∼75–130 μmol peptide or ∼2 μmol gp120.