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. Author manuscript; available in PMC: 2019 Mar 2.
Published in final edited form as: J Proteome Res. 2018 Feb 8;17(3):987–999. doi: 10.1021/acs.jproteome.7b00639

Figure 3. Ion mobility mass spectrometric analysis of BG505 SOSIP.v4.1-GT1 glycans.

Figure 3

Negative ion electrospray spectra of N-glycans enzymatically released from the gp120 subunit of CHO cell-produced BG505 SOSIP.v4.1-GT1 trimers. (A) Mobility-extracted singly charged negative ions found on gp120. The corresponding singly charged ions are encircled with the yellow oval in the DriftScope image (m/z against drift time) in Panel B. (B) Mobility extracted doubly charged negative ions found on gp120. The ions are encircled with a blue oval in the DriftScope image. (C–E) Collision-induced dissociation spectra for three distinct glycans derived from the transfer region of the Synapt G2Si instrument. The insets to panels C, D and E show the corresponding glycans as well as the numbering of the fragments. Panel E shows only the low mass region to emphasize the missing m/z 306 ion, the absence of which is diagnostic of α2,3-linked sialic acids (82). The numbering scheme follows that proposed elsewhere (83). The glycan symbols are shown on panel A. The complete glycan libraries of the SOSIP.664 and GT1 trimers are shown in Table S3.

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