The story of the Sda antigen and of its cognate enzyme B4GALNT2: What is new?

Duca, Martina; Malagolini, Nadia; Dall’Olio, Fabio

doi:10.1007/s10719-022-10089-1

Cited by 4 publications

(7 citation statements)

References 75 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The anti-SDa IgM was about 10-fold lower than anti-Gal IgM which is consistent with what is known about the SID blood group. 5,9,10 In 28 serum samples we detected evidence of IgM binding to one or more of the porcine proteins, predominantly CD46 and CD9 (Table 1). The level of antibody binding to porcine proteins was comparable, though much less frequent, to IgM binding to SDa (Figure 2B and C).…”

Section: Proteins Detected (N) Serummentioning

confidence: 98%

“…8 SID is a polyagglutinable blood group because most individuals have low levels of anti-SDa IgM which agglutinates red blood cells with high SDa levels. 5,9,10 Cells from pigs engineered with mutations to eliminate expression of the Gal, Neu5Gc, and SDa glycans, triple knockout pigs (TKO), show greatly reduced human antibody binding, with about 30% of patient samples showing no apparent reactivity. 11 Far less is known about the clinical potential for antibodies induced to porcine protein antigens.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Anti‐pig antibodies in swine veterinarian serum: Implications for clinical xenotransplantation

Byrne,

McGregor

2024

Xenotransplantation

View full text Add to dashboard Cite

Recent clinical xenotransplantation and human decedent studies demonstrate that clinical hyperacute rejection of genetically engineered porcine organs can be reliably avoided but that antibody mediated rejection (AMR) continues to limit graft survival. We previously identified porcine glycans and proteins which are immunogenic after cardiac xenotransplantation in non‐human primates, but the clinical immune response to antigens present in glycan depleted triple knockout (TKO) donor pigs is poorly understood. In this study we use fluorescence barcoded human embryonic kidney cells (HEK) and HEK cell lines expressing porcine glycans (Gal and SDa) or proteins (tetraspanin‐29 [CD9], membrane cofactor protein [CD46], protectin, membrane attack complex inhibition factor [CD59], endothelial cell protein C receptor, and Annexin A2) to screen antibody reactivity in human serum from 160 swine veterinarians, a serum source with potential occupational immune challenge from porcine tissues and pathogens. High levels of anti‐Gal IgM were present in all samples and lower levels of anti‐SDa IgM were present in 41% of samples. IgM binding to porcine proteins, primarily CD9 and CD46, previously identified as immunogenic in pig to non‐human primate cardiac xenograft recipients, was detected in 28 of the 160 swine veterinarian samples. These results suggest that barcoded HEK cell lines expressing porcine protein antigens can be useful for screening human patient serum. A comprehensive analysis of sera from clinical xenotransplant recipients to define a panel of commonly immunogenic porcine antigens will likely be necessary to establish an array of porcine non‐Gal antigens for effective monitoring of patient immune responses and allow earlier therapies to reverse AMR.

show abstract

Section: Proteins Detected (N) Serummentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Anti‐pig antibodies in swine veterinarian serum: Implications for clinical xenotransplantation

Byrne,

McGregor

2024

Xenotransplantation

View full text Add to dashboard Cite

show abstract

“…With the rules established so far, even such an exotic item can be named (Figure 9). The bladder protein uromodulin aka Tamm-Horsefall protein contains glycans with sulfated GalNAc and the Sd a determinant, which harbors a branch on the galactose residue [48,49]. Based on the rules for Lewis determinants, we use a round bracket embracing the two terminal residues, which do need linkage specifiers as GalNAc has only ever been found in β1-4 linkage.…”

Section: Special Structures In Brain and Bladdermentioning

confidence: 99%

Introduction of a human- and keyboard-friendly N-glycan nomenclature

Altmann,

Helm,

Pabst

et al. 2024

Beilstein J. Org. Chem.

View full text Add to dashboard Cite

In the beginning was the word. But there were no words for N-glycans, at least, no simple words. Next to chemical formulas, the IUPAC code can be regarded as the best, most reliable and yet immediately comprehensible annotation of oligosaccharide structures of any type from any source. When it comes to N-glycans, the venerable IUPAC code has, however, been widely supplanted by highly simplified terms for N-glycans that count the number of antennae or certain components such as galactoses, sialic acids and fucoses and give only limited room for exact structure description. The highly illustrative – and fortunately now standardized – cartoon depictions gained much ground during the last years. By their very nature, cartoons can neither be written nor spoken. The underlying machine codes (e.g., GlycoCT, WURCS) are definitely not intended for direct use in human communication. So, one might feel the need for a simple, yet intelligible and precise system for alphanumeric descriptions of the hundreds and thousands of N-glycan structures. Here, we present a system that describes N-glycans by defining their terminal elements. To minimize redundancy and length of terms, the common elements of N-glycans are taken as granted. The preset reading order facilitates definition of positional isomers. The combination with elements of the condensed IUPAC code allows to describe even rather complex structural elements. Thus, this “proglycan” coding could be the missing link between drawn structures and software-oriented representations of N-glycan structures. On top, it may greatly facilitate keyboard-based mining for glycan substructures in glycan repositories.

show abstract

“…O-glycosylation is intricately associated with cellular recognition, adhesion, immune response and other vital biological processes [ 2 ]. The B4GALNT2 gene is currently under extensive investigation for its involvement in animal immunology [ 1 , 3 , 4 ], gastrointestinal disorders [ 5 , 6 , 7 , 8 , 9 ], and its association with litter size. Additionally, B4GALNT2 has been identified as a potential candidate for the genetic regulation of Fec L mutations in sheep [ 10 ].…”

Section: Introductionmentioning

confidence: 99%

An Identification of Functional Genetic Variants in B4GALNT2 Gene and Their Association with Growth Traits in Goats

Xu,

Chen,

Chen

et al. 2024

Genes

View full text Add to dashboard Cite

β-1,4-N-acetylgalactosamine transferase 2 (B4GALNT2) is a vital candidate gene that affects the growth traits in sheep. However, whether it has the same function in goats remains to be investigated further. This study selected 348 Nanjiang Yellow goats, screened all exons, and conserved non-coding regions of the B4GALNT2 gene for single-nucleotide polymorphisms (SNPs). Our results revealed the presence of a synonymous mutation, rs672215506, within the exon of the B4GALNT2 gene in the Nanjiang Yellow goat population. The mutation resulted in a decrease in the mRNA stability of the B4GALNT2 gene. The results of SNP detection of the conserved non-coding region of the B4GALNT2 gene showed five potential regulatory SNPs in the Nanjiang Yellow goat population. Except for rs66095343, the ~500 bp fragments of the other four SNPs (rs649127714, rs649573228, rs652899012, and rs639183528) significantly increased the luciferase activity both in goat skeletal muscle satellite cells (MuSCs) and 293T cells. The genetic diversity indexes indicated low or intermediate levels for all six SNPs analyzed, and the genotype frequencies were in Hardy–Weinberg equilibrium. Association analysis showed that rs660965343, rs649127714, and rs649573228 significantly correlate with growth traits in the later stage of growth and development of Nanjiang Yellow goats. The haplotype combinations of H2H3 and H2H2 had higher body weight and greater body size. Moreover, H2H2 haplotype combinations significantly correlated with the litter size of the Nanjiang Yellow goats. The results of our study demonstrate the potential role of the B4GALNT2 gene as a functional genetic marker in the breeding programs of Nanjiang Yellow goats.

show abstract

The story of the Sda antigen and of its cognate enzyme B4GALNT2: What is new?

Cited by 4 publications

References 75 publications

Anti‐pig antibodies in swine veterinarian serum: Implications for clinical xenotransplantation

Anti‐pig antibodies in swine veterinarian serum: Implications for clinical xenotransplantation

Introduction of a human- and keyboard-friendly N-glycan nomenclature

An Identification of Functional Genetic Variants in B4GALNT2 Gene and Their Association with Growth Traits in Goats

Contact Info

Product

Resources

About