Plants have emerged as an alternative to current systems for the production of therapeutic proteins. Plants offer many potential benefits for the production of recombinant pharmaceutical proteins in terms of cost, scalability, and safety. A major advantage of plants is their ability to perform most of the PTMs that are required for the bioactivity and pharmacokinetics of recombinant therapeutic proteins. However, they are not able to reproduce human glycosylation perfectly. Several attractive strategies to humanize plant N -glycans have been proposed; in this context, fast analytical approaches are necessary for the analysis of protein glycosylation. Developments in MS are crucial for glycan analysis and should allow high-throughput structural analysis of N-glycans at the amounts available in plant proteomic studies. Fragmentation spectra can provide a great deal of information and in most cases should replace exo-glycosidase digestions. Extensive databases of MS/MS spectra should be available, and high-throughput tools to help glycobiologists to interpret MS/MS spectra should be essential in glycomics and glycoproteomics. The exoglycosidase digestions will probably only be used to help elucidate unusual glycan structures. On the glycopep-tide level, it is rather difficult to identify glycopeptides using MS in a complex protein digest. To overcome this problem, LAC is a very effective tool to target glycopep-tides and can be used to remove efficiently non-glycosylated peptides and concentrate glycopeptides for proteomic purposes. The uses of lectin-based chemistries for high sensitivity glycomic/glycoproteomic structural analysis are likely to grow. Q-TOF, Q-FTICR mass spectrometers, and ion trap mass spectrometers using the complementary techniques of CID and ETD are particularly versatile instruments for glycopeptide analysis and should be very useful to integrate glycosylation analysis into plant pro-teomics.
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