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. 2022 Mar 22;13:824746. doi: 10.3389/fimmu.2022.824746

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Copyright © 2022 Pothlichet, Meola, Bugault, Jeammet, Savitt, Ghebrehiwet, Touqui, Pouletty, Fiore, Sauvanet and Thèze

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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PLA2G1B directly binds to gp41. (A, B) gp41 binds to coated PLA2G1B by ELISA. Binding to coated PLA2G1B of serial dilutions (0-1 µg/well) of gp41 (D117III strain on A and MN strain on B), or unrelated proteins (CTL1: EFF-1 on A and B or CTL2: IF38 on A). (C, D) PLA2G1B binds to coated gp41 by ELISA. Binding of serial dilutions (0-1 µg/well) of PLA2G1B to coated gp41 (D117III on C, or MN on D) was tested in triplicate by ELISA. Results are shown as the mean ± SD of the OD value of one representative experiment among two (A), five (B), one (C) and five (D). (E) gp41 binds to PLA2G1B in pull-down assays. Recombinant PLA2G1B protein was incubated with strep-tagged-gp41 (D117III strain, gp41+PLA2G1B) or not (PLA2G1B only). PLA2G1B-gp41 complexes were pulled-down with strep-tactin XT-beads that pull-down gp41. Pulled-down products and unbound proteins were revealed by immunoblotting with goat polyclonal anti-gp41 Ab or mouse anti-PLA2G1B mAb. One representative experiment of five experiments with similar results with D117III gp41 is presented. Similar results were obtained in three experiments with MN gp41 ( Supplementary Figure 2 ).