TY - JOUR TI - Altered N-glycan composition impacts flagella-mediated adhesion in Chlamydomonas reinhardtii AU - Xu, Nannan AU - Oltmanns, Anne AU - Zhao, Longsheng AU - Girot, Antoine AU - Karimi, Marzieh AU - Hoepfner, Lara AU - Kelterborn, Simon AU - Scholz, Martin AU - Beißel, Julia AU - Hegemann, Peter AU - Bäumchen, Oliver AU - Liu, Lu-Ning AU - Huang, Kaiyao AU - Hippler, Michael A2 - Sengupta, Piali A2 - Yildiz, Ahmet A2 - Bloodgood, Robert A2 - Rico, Felix VL - 9 PY - 2020 DA - 2020/12/10 SP - e58805 C1 - eLife 2020;9:e58805 DO - 10.7554/eLife.58805 UR - https://doi.org/10.7554/eLife.58805 AB - For the unicellular alga Chlamydomonas reinhardtii, the presence of N-glycosylated proteins on the surface of two flagella is crucial for both cell-cell interaction during mating and flagellar surface adhesion. However, it is not known whether only the presence or also the composition of N-glycans attached to respective proteins is important for these processes. To this end, we tested several C. reinhardtii insertional mutants and a CRISPR/Cas9 knockout mutant of xylosyltransferase 1A, all possessing altered N-glycan compositions. Taking advantage of atomic force microscopy and micropipette force measurements, our data revealed that reduction in N-glycan complexity impedes the adhesion force required for binding the flagella to surfaces. This results in impaired polystyrene bead binding and transport but not gliding of cells on solid surfaces. Notably, assembly, intraflagellar transport, and protein import into flagella are not affected by altered N-glycosylation. Thus, we conclude that proper N-glycosylation of flagellar proteins is crucial for adhering C. reinhardtii cells onto surfaces, indicating that N-glycans mediate surface adhesion via direct surface contact. KW - N-glycosylation KW - cell adhesion KW - atomic force measurements KW - micropipette force measurements KW - Intraflagellar Transport KW - TIRF microscopy JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -