PT  - JOURNAL ARTICLE
AU  - Nannan Xu
AU  - Anne Oltmanns
AU  - Longsheng Zhao
AU  - Antoine Girot
AU  - Marzieh Karimi
AU  - Lara Hoepfner
AU  - Simon Kelterborn
AU  - Martin Scholz
AU  - Julia Beißel
AU  - Peter Hegemann
AU  - Oliver Bäumchen
AU  - Luning N. Liu
AU  - Kaiyao Huang
AU  - Michael Hippler
TI  - Altered <em>N</em>-glycan composition impacts flagella mediated adhesion in <em>Chlamydomonas reinhardtii</em>
AID  - 10.1101/2020.05.18.102624
DP  - 2020 Jan 01
TA  - bioRxiv
PG  - 2020.05.18.102624
4099  - http://biorxiv.org/content/early/2020/05/22/2020.05.18.102624.short
4100  - http://biorxiv.org/content/early/2020/05/22/2020.05.18.102624.full
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. It is unknown whether the composition of N-glycans attached to respective proteins is important for these processes. To this end, we examined several C. reinhardtii insertional mutants and a CRIPSR/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. In addition, polystyrene bead binding and transport is impaired. Notably, assembly, Intraflagellar Transport and FMG-1B transport 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.