Dataset Information

CD209L/L-SIGN N-Glycosylation and N-Glycosylation Site Occupancy

ABSTRACT: CD209L is a membrane glycoprotein with known glycan-binding properties and it also contains 2 N-glycosylation sequons at sites N92 and N361. Treatment with PNGase F in the presence of H218O, which removes N-linked glycans and isotopically labels the formerly-glycosylated site, confirmed that both unmodified and formerly-glycosylated versions of the peptide spanning the N92 N-glycosylated sequon were present. This suggests that a portion of CD209L protein is N-glycosylated at site N92. nUPLC-MS/MS analyses of CD209L digests enabled detection of a glycopeptide consistent with high-mannose type N-linked glycosylation.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Kevin Chandler

LAB HEAD: Catherine E Costello

PROVIDER: PXD021309 | Pride | 2021-09-09

REPOSITORIES: Pride

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Publications

CD209L/L-SIGN and CD209/DC-SIGN Act as Receptors for SARS-CoV-2.

Amraei Razie R Yin Wenqing W Napoleon Marc A MA Suder Ellen L EL Berrigan Jacob J Zhao Qing Q Olejnik Judith J Chandler Kevin Brown KB Xia Chaoshuang C Feldman Jared J Hauser Blake M BM Caradonna Timothy M TM Schmidt Aaron G AG Gummuluru Suryaram S Mühlberger Elke E Chitalia Vipul V Costello Catherine E CE Rahimi Nader N

ACS central science 20210630 7

As the COVID-19 pandemic continues to spread, investigating the processes underlying the interactions between SARS-CoV-2 and its hosts is of high importance. Here, we report the identification of CD209L/L-SIGN and the related protein CD209/DC-SIGN as receptors capable of mediating SARS-CoV-2 entry into human cells. Immunofluorescence staining of human tissues revealed prominent expression of CD209L in the lung and kidney epithelia and endothelia. Multiple biochemical assays using a purified reco ...[more]

PMID: 34341769

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Project description:As in animals, cell-cell communication plays pivotal role in male-female recognition during plant sexual reproduction. Prelaid peptides secreted from the female reproductive tissues guide pollen tubes towards ovules for fertilization. However, the elaborate mechanisms for this dialogue have remained elusive, particularly from the male perspective. We perform genome-wide quantitative liquid chromatography coupled tandem mass spectrometry of a pistil-stimulated pollen tube secretome and identify 801 pollen tube-secreted proteins. Interestingly, in silico analysis reveals that the pollen tube-secretome is dominated by unconventional-type secreted proteins representing 57% of the total secretome. In support, we show that unconventional-type protein, translationally controlled tumor protein, is secreted to the apoplast. Remarkably, we discover that this protein could be secreted by infiltrating through the initial phases of the conventional secretory pathway and could reach the apoplast via exosomes as demonstrated by co-localization with Oleisin1 exosome marker. We demonstrate that Arabidopsis thaliana translationally controlled tumor protein-knockdown plants have pollen tubes that poorly navigate to the target ovule, and theÂ knocked down allele is poorly transmitted through the male. We show that regulators of the endoplasmic reticulum-trans-golgi network protein secretory pathway control secretion of pollen tube-secreted cysteine-rich proteins, including pollen tube attractants, and are essential for pollen tube growth and guidance, as well as ovule-targeting competence. This work, the first pollen tube secretome study, identifies novel genome-wide pollen tube-secreted proteins with potential function in pollen tube-ovule guidance for sexual reproduction. Functional analysis highlights a potential mechanism for pollen tube unconventional protein secretion and reveals likely regulators of pollen tube protein secretion. The association of pollen tube-secreted proteins with marker proteins shown to be secreted via exosomes in other species suggest secretion via exosomes as a possible mechanism for cell-cell communication between the pollen tube and female reproductive cells. For processed dataset with quantitative information, see Hafidh S, Potesil D, Fila J et al. Genome Bilogy 2016.

Dataset Information

CD209L/L-SIGN N-Glycosylation and N-Glycosylation Site Occupancy

Publications

CD209L/L-SIGN and CD209/DC-SIGN Act as Receptors for SARS-CoV-2.

Similar Datasets

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