Correction to: Scientific Reports https://doi.org/10.1038/s41598-022-26532-0, published online 05 January 2023
The original version of this Article contained an error in the legend of Figure 2.
“(A) SDS-PAGE of C. hepaticus HV10T, C. jejuni 354, C. coli 52/2 and C. upsaliensis 54/7 whole cell lysates (WCL) containing 25 µg of protein. (B) SBA lectin blot binding profiles to N-glycans present in WCL of C. hepaticus HV10T, C. jejuni 354, C. coli 52/2, C. upsaliensis 54/7 containing 25 µg of protein. (C) SDS-PAGE of C. lari 54/6, C. fetus 54/3 alongside negative controls, S. Typhimurium PT44. The equivalent amount of protein from WCL of the different Campylobacter species were also digested with proteinase K (P.K).Whole cell lysates were separated by 8–16% SDS-PAGE and either developed with SimplyBlue™ SafeStain or transferred to PVDF membranes for blotting. (D) SBA lectin blot binding profiles to N-glycans present in WCL of C. lari 54/6, C. fetus 54/3, C. coli 52/2, E. coli JM109 and S. Typhimurium PT44 containing 25 µg of protein.”
now reads:
“(A) SDS-PAGE of C. hepaticus HV10T, C. jejuni 354, C. coli 52/2 and C. upsaliensis 54/7 whole cell lysates (WCL) containing 25 µg of protein. (B) SBA lectin blot binding profiles to N-glycans present in WCL of C. hepaticus HV10T, C. jejuni 354, C. coli 52/2, C. upsaliensis 54/7 containing 25 µg of protein. (C) SDS-PAGE of C. lari 54/6, C. fetus 54/3 alongside negative control, S. Typhimurium PT44. The equivalent amount of protein from WCL of the different Campylobacter species were also digested with proteinase K (P.K).Whole cell lysates were separated by 8–16% SDS-PAGE and either developed with SimplyBlue™ SafeStain or transferred to PVDF membranes for blotting. (D) SBA lectin blot binding profiles to N-glycans present in WCL of C. lari 54/6, C. fetus 54/3 and S. Typhimurium PT44 containing 25 µg of protein.”
Additionally, the original version of this Article contained errors in the legend of Figure 5.
“Ion-trap CID-MS spectra of two C. hepaticus HV10T glycopeptides. Spectra represent fragmented ions produced from the N-glycan. (A) C. hepaticus HV10T glycopeptide 23IQGTIAQIYDNNK36 with a delta mass of 1405.56 Da. (B) C. hepaticus HV10T glycopeptide 266AALAEGEANATIISAK282 with a delta mass of 1405.56 Da. Above is the heptasaccharide structure linked to the peptide drawn using the symbol nomenclature for glycans SNFG. The MS/MS spectra display fragmented ions generated from the glycan with the structure HexNAc-HexHAc-[Hex]-HexNAc-HexHAc-HexNAc-diNAcBac.”
now reads:
“Ion-trap CID-MS spectra of two C. hepaticus HV10T glycopeptides. Spectra represent fragmented ions produced from the N-glycan. (A) C. hepaticus HV10T glycopeptide 266AALAEGEANATIISAK282 with a delta mass of 1405.56 Da. (B) C. hepaticus HV10T glycopeptide 23IQGTIAQIYDNNK36 with a delta mass of 1405.56 Da. Above is the heptasaccharide structure linked to the peptide drawn using the symbol nomenclature for glycans SNFG. The MS/MS spectra display fragmented ions generated from the glycan with the structure HexNAc-HexHAc-[Hex]-HexNAc-HexHAc-HexNAc-diNAcBac.”
The original Article has been corrected.
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McDonald, J.B., Scott, N.E., Underwood, G.J. et al. Author Correction: Characterisation of N-linked protein glycosylation in the bacterial pathogen Campylobacter hepaticus. Sci Rep 14, 9490 (2024). https://doi.org/10.1038/s41598-024-59808-8
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DOI: https://doi.org/10.1038/s41598-024-59808-8
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