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February 2017

Volume 16Issue 2p146-326
Open Access
On the cover: Anti-citrullinated protein antibodies (ACPA) isolated from rheumatoid arthritis (RA) patients are extensively Fabglycosylated. The structural analyses revealed that ACPA-IgG molecules contain highly sialylated glycans in their Fab-domain. Importantly, Fab-glycans were estimated to be present on over 90% of ACPA-IgG. These observations provide the first evidence pointing to the ability of ACPA-IgG to mediate novel immunological activities via their hyper-sialylated Fab-glycans. For details, see the article by Lise Hafkenscheid, et al., pages 278–287....
On the cover: Anti-citrullinated protein antibodies (ACPA) isolated from rheumatoid arthritis (RA) patients are extensively Fabglycosylated. The structural analyses revealed that ACPA-IgG molecules contain highly sialylated glycans in their Fab-domain. Importantly, Fab-glycans were estimated to be present on over 90% of ACPA-IgG. These observations provide the first evidence pointing to the ability of ACPA-IgG to mediate novel immunological activities via their hyper-sialylated Fab-glycans. For details, see the article by Lise Hafkenscheid, et al., pages 278–287.

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