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ABSTRACT Cholera toxin (CT) is the etiological agent of cholera. Here we report that multiple classes of fucosylated glycoconjugates function in CT binding and intoxication of intestinal

epithelial cells. In Colo205 cells, knockout (KO) of _B3GNT5_, which encodes an enzyme required for synthesis of lacto and neolacto series glycosphingolipids (GSLs), reduces CT binding but

sensitizes cells to intoxication. Overexpressing _B3GNT5_ to generate more fucosylated GSLs confers protection against intoxication, indicating that fucosylated GSLs act as decoy receptors

for CT. KO of _B3GALT5_ causes increased production of fucosylated _O_-linked and _N_-linked glycoproteins and leads to increased CT binding and intoxication. KO of _B3GNT5_ in _B3GALT5_-KO

cells eliminates production of fucosylated GSLs but increases intoxication, identifying fucosylated glycoproteins as functional receptors for CT. These findings provide insight into the

molecular determinants regulating CT sensitivity of host cells. Access through your institution Buy or subscribe This is a preview of subscription content, access via your institution ACCESS

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FAQs * Contact customer support SIMILAR CONTENT BEING VIEWED BY OTHERS _PAENICLOSTRIDIUM SORDELLII_ HEMORRHAGIC TOXIN TARGETS TMPRSS2 TO INDUCE COLONIC EPITHELIAL LESIONS Article Open access

26 July 2022 CHARACTERIZATION AND UTILITY OF TWO MONOCLONAL ANTIBODIES TO CHOLERA TOXIN B SUBUNIT Article Open access 15 March 2023 CLIC AND MEMBRANE WOUND REPAIR PATHWAYS ENABLE PANDEMIC

NOROVIRUS ENTRY AND INFECTION Article Open access 28 February 2023 DATA AVAILABILITY Data used to generate Fig. 1b,d are available from the Gene Expression Omnibus under accession number

GSE242156. MS data used to generate Fig. 3a, Extended Data Fig. 4a–d, Fig. 4a, Extended Data Fig. 7a–c, Extended Data Fig. 8a–c and Extended Data Fig. 6a are available from GlycoPOST under

accession number GPST000467. MS data used to generate Extended Data Fig. 6b,c are available from GlycoPOST under accession number GPST000465. Replicate immunoblot and lectin blot data are

available from the Texas Data Repository (https://doi.org/10.18738/T8/N9NF8B). Source data are provided with this paper. REFERENCES * Grant, T. A., Balasubramanian, D. & Almagro-Moreno,

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spectrometry of neutral underivatized oligosaccharides. _Anal. Chem._ 73, 651–657 (2001). Article  CAS  PubMed  Google Scholar  Download references ACKNOWLEDGEMENTS We thank A. Singla, D.

Andrade Silva and M. Burns for comments on the manuscript. We thank E. Capota and D. Andrade Silva for technical support. We thank A. Wands, D. Carroll, H. Wu, H. Khan and M. Shiloh for

advice and reagents. We thank the UT Southwestern Proteomics Core Facility and its director, A. Lemoff. We acknowledge support from the National Institutes of Health (R01GM090271 and

R35GM145599 to J.J.K. and R24GM137782 to P.A.), the Swedish Cancer Foundation (22 2079 Pj to S.T.) and the Welch Foundation (I-1686 to J.J.K.). M.T.G. received support from the NIH

(T32GM145467). We thank C. Cairo (University of Alberta) for the RhtrECI plasmid and R. Schnaar (Johns Hopkins) for the P4 inhibitor. AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Department

of Biochemistry, UT Southwestern Medical Center, Dallas, TX, USA Atossa C. Ghorashi, Rohit Sai Reddy Konada & Jennifer J. Kohler * Department of Microbiology and Immunology, Institute

of Biomedicine, University of Gothenburg, Gothenburg, Sweden Andrew Boucher & Ulf Yrlid * Complex Carbohydrate Research Center, The University of Georgia, Athens, GA, USA Stephanie A.

Archer-Hartmann, Mehrnoush Taherzadeh Ghahfarrokhi, Nathan B. Murray & Parastoo Azadi * Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, University of

Gothenburg, Gothenburg, Sweden Dani Zalem & Susann Teneberg * McDermott Center for Human Growth and Development, UT Southwestern Medical Center, Dallas, TX, USA Xunzhi Zhang & Chao

Xing * Department of Bioinformatics, UT Southwestern Medical Center, Dallas, TX, USA Chao Xing Authors * Atossa C. Ghorashi View author publications You can also search for this author

inPubMed Google Scholar * Andrew Boucher View author publications You can also search for this author inPubMed Google Scholar * Stephanie A. Archer-Hartmann View author publications You can

also search for this author inPubMed Google Scholar * Dani Zalem View author publications You can also search for this author inPubMed Google Scholar * Mehrnoush Taherzadeh Ghahfarrokhi View

author publications You can also search for this author inPubMed Google Scholar * Nathan B. Murray View author publications You can also search for this author inPubMed Google Scholar *

Rohit Sai Reddy Konada View author publications You can also search for this author inPubMed Google Scholar * Xunzhi Zhang View author publications You can also search for this author

inPubMed Google Scholar * Chao Xing View author publications You can also search for this author inPubMed Google Scholar * Susann Teneberg View author publications You can also search for

this author inPubMed Google Scholar * Parastoo Azadi View author publications You can also search for this author inPubMed Google Scholar * Ulf Yrlid View author publications You can also

search for this author inPubMed Google Scholar * Jennifer J. Kohler View author publications You can also search for this author inPubMed Google Scholar CONTRIBUTIONS A.C.G. and J.J.K.

conceptualized the project and experimental approach, with input from A.B., R.S.R.K. and U.Y. A.C.G. conducted all cell culture experiments, flow cytometry experiments, functional assays and

immunoblot experiments. A.B. prepared biotinylated CTB and CTB mutants with supervision from U.Y. S.A.A.-H. conducted MS analysis of intact glycolipids with supervision from P.A. M.T.G.

performed MS analysis of procainamide-labeled glycans from glycolipids with supervision from P.A. D.Z. isolated neutral glycolipids and conducted MS analysis of their glycans with

supervision from S.T. N.B.M. and S.A.A.-H. conducted _N_-linked and _O_-linked glycomic analyses with supervision from P.A. R.S.R.K. prepared EGCase and conducted preliminary analyses of

glycolipids. X.Z. performed bioinformatics analyses with supervision from C.X. A.C.G. and J.J.K. wrote the manuscript with input from all authors. CORRESPONDING AUTHOR Correspondence to

Jennifer J. Kohler. ETHICS DECLARATIONS COMPETING INTERESTS The authors declare no competing interests. PEER REVIEW PEER REVIEW INFORMATION _Nature Chemical Biology_ thanks the anonymous

reviewers for their contribution to the peer review of this work. ADDITIONAL INFORMATION PUBLISHER’S NOTE Springer Nature remains neutral with regard to jurisdictional claims in published

maps and institutional affiliations. EXTENDED DATA EXTENDED DATA FIG. 1 CHARACTERIZATION OF _B3GALT5-_KO AND _B3GALT5-_KO + OE CELLS. (A, B) Representative histograms (left panel) from the

flow cytometry analyses of cell surface binding of Lewis a antibody (A) or Lewis x antibody (B) to indicated cell lines. Bar graphs (right panel) show quantification from 3 independent

trials. Error bars indicate mean ± SD. (C) Quantification of gMFI from flow cytometry analyses of cells treated with increasing concentrations of CTB. Data shown are from 3 independent

trials and normalized to the maximum APC signal in WT cells. Error bars indicate mean ± SD. Indicated cell lines were incubated for 72 h with increasing concentrations of CTB-Saporin (D) or

unconjugated saporin (E). Cell survival upon internalization of CTB-saporin was measured using the Cell Titer-Glo 2.0 assay. Data shown are luminescence values normalized to the signal from

the untreated condition for each cell type. Each datapoint is a biological replicate consisting of 3 averaged technical replicates. Error bars indicate mean ± SD of 3 biological replicates.

(F) Cells pretreated with BFA or vehicle control for 0.5 h were incubated for 1.5 h with CT (1 nM) or buffer alone. Accumulation of cAMP was measured. Data shown are inverse of luminescence

values normalized first to the total amount of cells plated for each cell line, then to the signal in CT-treated control cells. Each datapoint is a biological replicate consisting of 3

averaged technical replicates. Error bars indicate mean ± SD of 3 biological replicates. (G) Control, _B3GALT5-_KO m1, m2 and KO + OE cells were treated with forskolin (10 µM) for 0.5 h and

then analyzed as in panel F. Statistical analyses for panels A and B were performed by one-way ANOVA with Tukey correction and for panels C, F, and G by two-way ANOVA with Tukey

correction.‘ns’ indicates not significant, **** indicates adjusted _P_-value < 0.0001. Exact _P_-values are as follows: 0.0004 and 0.0412 for control versus _B3GALT5-_KO m2 and

_B3GALT5-_KO + OE; 0.0041 and 0.0024 for _B3GALT5-_KO m1 versus _B3GALT5-_KO m2 and _B3GALT5-_KO + OE, respectively (panel B); 0.0390 for control versus _B3GALT5-_KO m2 treated with 0.0375 

μg/mL; 0.0002 and 0.0014 for control versus _B3GALT5-_KO m2 or m1 treated with 0.075 μg/mL, respectively (panel C). Source data EXTENDED DATA FIG. 2 CHARACTERIZATION OF _B3GNT5_-KO AND

_B3GNT5_-KO + OE CELLS. (A) Quantification of gMFI from flow cytometry analyses of cells treated with increasing concentrations of CTB. Data shown are from 3 independent trials and

normalized to the maximum APC signal in WT cells. Error bars indicate mean ± SD. (B, C) Representative histograms (left panel) from the flow cytometry analyses of cell surface binding of

Lewis x antibody (B) or Lewis a antibody (C) to control, _B3GNT5_-KO m1, m2 and KO + OE cells. Bar graphs (right panel) show quantification from 3 independent trials. Control, _B3GNT5_-KO m1

and KO + OE cells were incubated for 72 h with increasing concentrations of CTB-Saporin (D) or unconjugated saporin (E). Cell survival upon internalization of CTB-saporin was measured using

the Cell Titer-Glo 2.0 assay. Data shown are luminescence values normalized to the signal from the untreated condition for each cell type. Each datapoint is a biological replicate

consisting of 3 averaged technical replicates. Error bars indicate mean ± SD of 3 biological replicates. (F) Cells pretreated with BFA or a vehicle control for 0.5 h were incubated for 1.5 h

with CT (1 nM) or buffer alone. Accumulation of cAMP was measured. Data shown are inverse of luminescence values normalized first to the total amount of cells plated for each cell line,

then to the signal in CT-treated control cells. Each datapoint is a biological replicate consisting of 3 averaged technical replicates. Error bars indicate mean ± SD of 3 biological

replicates. (G) Control, _B3GNT5_-KO m1, m2 and KO + OE cells were treated with forskolin (10 µM) for 0.5 h and then analyzed as in panel F. Statistical analyses for panels B and C were

performed by one-way ANOVA with Tukey correction and for panels A, D, E, F, and G by two-way ANOVA with Tukey correction. ‘ns’ indicates not significant, **** indicates adjusted _P_-value 

< 0.0001. Exact _P_-values are as follows: 0.0219 for control versus _B3GNT5_-KO m1 treated with 1.25 μg/mL; 0.0010 and 0.0077 for control versus _B3GNT5_-KO m1 or m2 treated with 2.5 

μg/mL, respectively (panel A); 0.0059 and 0.0036 for control versus _B3GNT5_-KO + OE treated with 2.5 or 12.5 μg/mL CTB-saporin (panel D). Source data EXTENDED DATA FIG. 3 CHARACTERIZATION

OF _B3GALT5_ + _B3GNT5_-DKO CELLS. (A) Representative histograms (left panel) from the flow cytometry analyses of cell surface binding of Lewis x antibody to control, _B3GALT5_ -KO m1,

_B3GNT5_-KO m1, and _B3GALT5_ + _B3GNT5_-dKO cells. Bar graph (right panel) shows quantification from 3 independent trials. (B, C) Control, _B3GALT5-_KO m1, and _B3GALT5_ + _B3GNT5_-dKO

cells were incubated for 72 h with increasing concentrations of CTB-Saporin (B) or unconjugated saporin (C). Cell survival upon internalization of CTB-saporin measured using the Cell

Titer-Glo 2.0 assay. Data shown are luminescence values normalized to the signal from the untreated condition for each cell type. Each datapoint is a biological replicate consisting of 3

averaged technical replicates. Error bars indicate mean ± SD of 3 biological replicates. (D) Cells pretreated with BFA or a vehicle control for 0.5 h were incubated for 1.5 h with CT (1 nM)

or buffer alone. Accumulation of cAMP was measured. Data shown are inverse of luminescence values normalized first to the total amount of cells plated for each cell line, then to the signal

in CT-treated control cells. Each datapoint is a biological replicate (n = 2) consisting of 3 averaged technical replicates. (E) Control, _B3GALT5-_KO m1, m2 and KO + OE cells were treated

with forskolin (10 µM) for 0.5 h and then analyzed as in panel D. Each datapoint is a biological replicate consisting of 3 averaged technical replicates. Error bars indicate mean ± SD of 3

biological replicates. Statistical analyses for panel A were performed by one-way ANOVA with Tukey correction and for panels B, C, D, and E by two-way ANOVA with Tukey correction. ****

indicates adjusted _P_-value < 0.0001. Exact _P_-values are as follows: 0.0003 and 0.0048 for _B3GALT5_ + _B3GNT5_-dKO versus control or _B3GALT5-_KO m1, respectively (panel A); 0.0002

and 0.0171 for control versus _B3GALT5_ + _B3GNT5_-dKO treated with 2.5 μg/mL CTB saporin or 12.5 μg/mL saporin (panels C and D, respectively). Source data EXTENDED DATA FIG. 4 FUCOSYLATED

LACTO-SERIES GSLS DETECTED IN CONTROL BUT NOT KO CELL LINES. MS analysis of GSLs from control (A), _B3GALT5-_KO m1 (B), and _B3GNT5_-KO m1 (C) cells. (D) Example MS/MS spectrum of a

fucosylated lacto-series glycolipid detected in control cells, confirming structure. EXTENDED DATA FIG. 5 VALIDATION OF GSLS AS DECOY RECEPTORS FOR CT. (A) Lectin blot with CTB-biotin of

control and _B3GALT5_-KO m1 cell lysates, and pure GM1. Samples were treated for 16 h with endoglycoceramidase or a vehicle control. Data shown are a single representative trial of 3

independent biological replicates. (B-G) Control, _B3GNT5_-KO + OE, and _B3GALT5-_KO m1 cells were treated with P4 inhibitor of glycosphingolipid biosynthesis for 72 h then lysed for lectin

blot analysis (B) or treated with BFA or a vehicle control for 0.5 h prior to incubation with CT (1 nM) for analysis of cAMP accumulation (C, D, and E). Alternately, cells were treated with

forskolin (10 µM) for 0.5 h (F and G). Accumulation of cAMP was measured. Data shown are inverse of luminescence values normalized first to the total amount of cells plated for each cell

line, then to the signal in CT-treated control cells. Each datapoint is a biological replicate (n = 2 in panel E, n = 3 in panels C, D, F, and G) consisting of 3 averaged technical

replicates. Error bars indicate mean ± SD of 3 biological replicates. Statistical analyses were performed by two-way ANOVA with Tukey correction. Exact _P_-values are 0.0002 for control

versus inhibitor-treated _B3GALT5-_KO m1 as well as inhibitor-treated control versus untreated _B3GALT5-_KO m1; for inhibitor-treated control versus inhibitor-treated _B3GALT5-_KO m1, the

exact _P_-value is 0.0052 (panel C). Source data EXTENDED DATA FIG. 6 ANALYSIS OF GSLS FROM _B3GNT5_-KO + OE CELLS. (A) Glycolipids were isolated from _B3GALT5_-KO m1 or _B3GNT5_-KO + OE

cells. Glycans were released with endoglycoceramidase, labeled with procainamide, and analyzed by mass spectrometry with HILIC-FL separation. (B, C) LC-ESI/MS analysis of oligosaccharides

obtained by digestion of neutral GSLs from _B3GNT5_-KO + OE cells with endoglycoceramidase I. Diagnostic ions indicate carbohydrate linkage positions. (C) An MS spectrum displaying a series

of C type fragment ions (C2α at _m/z_ 528, C3α at _m/z_ 690, C4α at _m/z_ 1039, C5α at _m/z_ 1201, C6 at _m/z_ 1550, and C7 at _m/z_ 1712), which identified an oligosaccharide with

Hex-(Fuc-)HexNAc-Hex-(Fuc-)HexNAc-Hex-(Fuc-)HexNAc-Hex-Hex sequence. The ion at _m/z_ 364 is obtained by double glycosidic cleavage of the 3-linked branch (C2/Z3β), and characteristic for an

internal 4-linked GlcNAc substituted with a Fuc at 3-position that is a terminal Lex (refs. 90,94). Taken together this indicated an undecasaccharide with a terminal Lex determinant. (D, E)

_B3GALT5_ + _B3GNT5_-dKO cells were incubated with GSLs extracted from _B3GNT5_-KO + OE cells, a commercial mixture of neutral GSLs, or purified GM1. Cells were then treated with BFA or a

vehicle control for 0.5 h prior to incubation with CT (1 nM) for analysis of cAMP accumulation (D). Alternately, cells were treated with forskolin (10 µM) for 0.5 h (n = 2) (E). Accumulation

of cAMP was measured. Data shown are inverse of luminescence values normalized first to the total amount of cells plated for each cell line, then to the signal in CT-treated control cells.

Each datapoint is a biological replicate (n = 3 for panel D, n = 2 for panel E) consisting of 2 averaged technical replicates. Error bars indicate mean ± SD of 3 biological replicates (panel

D). Statistical analyses were performed by two-way ANOVA with Tukey correction. No significant differences were observed. Source data EXTENDED DATA FIG. 7 _B3GALT5_-KO CELLS EXHIBIT

INCREASED FUCOSYLATION ON _N_-LINKED GLYCOPROTEINS. (A) _N_-linked glycoforms detected in control and _B3GALT5-_KO m1 cells by LC-MS/MS analysis. Quantification is based on triplicate

analysis. (B) Example MS/MS of a complex, fucosylated _N_-linked glycan detected in _B3GALT5_-KO m1 cells confirming placement of fucose. (C) Bar graphs showing the relative enrichment of

mono- vs di- vs tri-fucosylated _N_-linked glycans detected by LC-MS/MS analysis of control and _B3GALT5-_KO m1 cells. Statistical analysis was performed by two-tailed t-test with Holm-Šídák

correction. Exact adjusted _P_-value = 0.013508 for mono-fucosylated _N_-linked glycans detected in control versus _B3GALT5-_KO m1. Exact adjusted _P_-value = 0.014105 for both di- and

tri-fucosylated _N_-linked glycans detected in _B3GALT5-_KO m1 versus control. EXTENDED DATA FIG. 8 _B3GALT5-_KO CELLS EXHIBIT INCREASED FUCOSYLATION ON _O_-LINKED GLYCOPROTEINS. (A)

_O_-linked glycoforms detected in control and _B3GALT5-_KO m1 cells by LC-MS/MS analysis. Quantification is based on triplicate analysis. (B) Example MS/MS of a fucosylated _O_-linked glycan

detected in _B3GALT5_-KO m1 cells. (C) Example MS/MS of core 2 _O_-linked glycan detected in _B3GALT5-_KO m1 cells confirming structure. (D, E) _B3GALT5-_KO m1 cells were rescued with

either WT or catalytically dead (mut) _B3GALT5-_OE. Rescued cells were treated with BFA or a vehicle control for 0.5 h prior to incubation with CT (1 nM) for analysis of cAMP accumulation

(D). Alternately, cells were treated with forskolin (10 µM) for 0.5 h (E). Accumulation of cAMP was measured. Data shown are inverse of luminescence values normalized first to the total

amount of cells plated for each cell line, then to the signal in CT-treated control cells. Each datapoint is a biological replicate consisting of 2 averaged technical replicates. Error bars

indicate mean ± SD of 3 biological replicates. Statistical analyses were performed by two-way ANOVA with Tukey correction. No significant differences were observed. Source data EXTENDED DATA

FIG. 9 VALIDATION OF _SLC35C1-_KO CELL LINES. (A) GM1 was treated with EGCase or vehicle, then detected by lectin blot using WT CTB-biotin, W88K CTB-biotin, and H18L CTB-biotin. Data

presented are from 3 distinct membranes processed simultaneously (separated by vertical lines) and are a single representative trial from 3 biological replicates. (B, C) Representative

histograms (left panel) from flow cytometry analyses of anti-Lex antibody (B) and AAL (C) binding to surfaces of control, _B3GALT5-_KO m1, _SLC35C1-_KO, and _B3GALT5_ + _SLC35C1-_dKO cells.

Quantification of gMFIs (right panel) from 3 biological replicates are normalized to the maximum signal in control cells. Lysates from control, _B3GALT5-_KO m1, _SLC35C1-_KO and _B3GALT5_ + 

_SLC35C1_-dKO cells were analyzed by immunoblot probing with anti-Lex antibody or lectin blot probing with AAL (D). Data shown are a single representative trial from 3 biological replicates.

(E) Control, _B3GALT5-_KO m1, _SLC35C1-_KO and _B3GALT5_ + _SLC35C1-_dKO cells were incubated for 72 h with unconjugated saporin (12.5 μg/mL). Survival data shown are luminescence values

normalized to the signal from the untreated condition for each cell type. Each datapoint indicates the mean of 2 biological replicates, each consisting of 3 averaged technical replicates.

(F) Cells pretreated with BFA or a vehicle control for 0.5 h were incubated for 1.5 h with CT (1 nM) or buffer alone. Accumulation of cAMP was measured. Data shown are inverse of

luminescence values normalized first to the total amount of cells plated for each cell line, then to the signal in CT-treated control cells. Each datapoint is a biological replicate (n = 2)

consisting of 3 averaged technical replicates. (G) Cells were treated with forskolin (10 µM) for 0.5 h and then analyzed as in panel F. Each datapoint is a biological replicate consisting of

3 averaged technical replicates. Error bars indicate mean ± SD of 3 biological replicates. Statistical analyses were performed by one-way (panels B and C) or two-way (panels F and G) ANOVA

with Tukey correction. **** indicates adjusted _P_-value < 0.0001. Exact _P_-value for control versus _B3GALT5-_KO m1 treated with AAL is 0.0018. Source data EXTENDED DATA FIG. 10

CTB-INTERACTING GLYCOPROTEINS. (A) Top 50 proteins identified from CTB-biotin pulldown from _B3GALT5_ + _B3GNT5_-dKO versus _B3GALT5_ + _SLC35C1-_dKO cell lysates. Fold-change is the

abundance in the _B3GALT5_ +  _B3GNT5_-dKO pulldown as compared to the _B3GALT5_ + _SLC35C1-_dKO pulldown. Unadjusted _P_-values are derived from two-tailed student’s t-test. (B) Gene

ontology (GO) analysis using Fisher’s exact test with Bonferroni correction to identify pathways enriched in CTB-biotin pulldown from _B3GALT5_ + _B3GNT5-_dKO cell lysates as compared to

_B3GALT5_ + _SLC35C1-_dKO cell lysates. Top 25 pathways are shown. (C) Two hits (FLOT1 and MUC1, boldface font in panel A) were selected for confirmation. Total lysates and material from

CTB-biotin pulldowns were analyzed by immunoblot using antibodies against FLOT1 and MUC1. Source data SUPPLEMENTARY INFORMATION SUPPLEMENTARY INFORMATION Supplementary Fig. 1. REPORTING

SUMMARY SUPPLEMENTARY TABLE 1 Reagents list. SUPPLEMENTARY TABLE 2 Oligonucleotide list. SUPPLEMENTARY TABLE 3 CRISPR KO sequence validation. SOURCE DATA SOURCE DATA FIG. 1 Statistical

source data. SOURCE DATA FIG. 2 Statistical source data. SOURCE DATA FIG. 3 Statistical source data. SOURCE DATA FIG. 4 Statistical source data. SOURCE DATA FIG. 5 Statistical source data.

SOURCE DATA FIG. 6 Statistical source data. SOURCE DATA EXTENDED DATA FIG. 1 Statistical source data. SOURCE DATA EXTENDED DATA FIG. 2 Statistical source data. SOURCE DATA EXTENDED DATA FIG.

3 Statistical source data. SOURCE DATA EXTENDED DATA FIG. 5 Statistical source data. SOURCE DATA EXTENDED DATA FIG. 6 Statistical source data. SOURCE DATA EXTENDED DATA FIG. 8 Statistical

source data. SOURCE DATA EXTENDED DATA FIG. 9 Statistical source data. SOURCE DATA EXTENDED DATA FIG. 9 Uncropped western blot. SOURCE DATA EXTENDED DATA FIG. 10 Uncropped western blot.

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permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Ghorashi, A.C., Boucher, A., Archer-Hartmann, S.A. _et al._ Fucosylation of glycoproteins and glycolipids: opposing roles in cholera

intoxication. _Nat Chem Biol_ 21, 555–566 (2025). https://doi.org/10.1038/s41589-024-01748-5 Download citation * Received: 08 August 2023 * Accepted: 13 September 2024 * Published: 16

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