Author: Bederka, Lydia H.; Bonhomme, Cyrille J.; Ling, Emily L.; Buchmeier, Michael J.
Title: Arenavirus Stable Signal Peptide Is the Keystone Subunit for Glycoprotein Complex Organization Document date: 2014_10_28
ID: wbh06gzb_16
Snippet: Immunoprecipitation of SSP by using HA agarose beads retained its association with the GP2 subunit. The wild-type HA SSP GPC immunoprecipitation results, containing only the inserted HA epitope with no point mutations, revealed the interaction with the GP2 subunit (Fig. 6B, lane 6) . The HA SSP GPC 49A mutant did not allow for glycoprotein processing; thus, there was no detectable GP2 (Fig. 6B, lane 7) . HA SSP GPC 49Y and HA SSP GPC 50A point mu.....
Document: Immunoprecipitation of SSP by using HA agarose beads retained its association with the GP2 subunit. The wild-type HA SSP GPC immunoprecipitation results, containing only the inserted HA epitope with no point mutations, revealed the interaction with the GP2 subunit (Fig. 6B, lane 6) . The HA SSP GPC 49A mutant did not allow for glycoprotein processing; thus, there was no detectable GP2 (Fig. 6B, lane 7) . HA SSP GPC 49Y and HA SSP GPC 50A point mutants also resulted in varied GP2 subunit immunoprecipitation (Fig. 6B, lanes 8 and 9) . The HA SSP GPC 52A sample, as well as FALA GPC and YALL GPC, did not reveal any GP2 pulldown product (Fig. 6B, lanes 10 to 12) . FALA GPC and YALL GPC did not contain HA epitope expression for successful immunoprecipitation and served as additional agarose bead controls.
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