EC Number   |
General Information |
Reference |
|---|
  2.4.1.B69 | evolution |
genotyping, overview. The variable presence of two open reading frames (ORFs) in the pgl locus includes a putative glycosyltransferase gene, pglG, in addition to a glucosyltransferase-expressing gene, pglH. Strains lacking these two ORFs retain the first 40 bp of pglG and the last 100 bp of pglH. Homologous recombination within the pgl loci, through genomic analysis of 100 African serogroup A isolates in Ethiopia in 2014, is detected representing the clonal replacement of hypervirulent meningococcal clone sequence type 7 (ST-7) by the ST-2859 descendant clone. Major polymorphism in pgl gene content within a small geographic area. This recombination event seems to emphasizes the role of protein glycosylation diversity in immune evasion. Although pglG is not shown to be functional in meningococci, the phase-variable poly(C) tract consists of 8 to 15 cytosines (Cs) and is presumably in the on and off configurations in 55 and 20 isolates (20 and 5 pairs), respectively. Fourteen of the paired isolates have a change of poly(G) tract length, and 7 of these result in a switch in predicted on/off status. The pglG gene is turned off in five of these individuals, and the pglG gene is turned on in two individuals |
759430 |
| 2.4.1.B69 | evolution |
genotyping, overview. The variable presence of two open reading frames (ORFs) in the pgl locus includes a putative glycosyltransferase gene, pglG, in addition to a glucosyltransferase-expressing gene, pglH. Strains lacking these two ORFs retain the first 40 bp of pglG and the last 100 bp of pglH. Homologous recombination within the pgl loci, through genomic analysis of 100 African serogroup A isolates in Ethiopia in 2014, is detected representing the clonal replacement of hypervirulent meningococcal clone sequence type 7 (ST-7) by the ST-2859 descendant clone. Major polymorphism in pgl gene content within a small geographic area. This recombination event seems to emphasizes the role of protein glycosylation diversity in immune evasion. Polymorphisms exist at the gene level described for pglH and pglH2, where only one nonsynonymous mutation is accountable for the glycoform switch from Glc to GlcNAc. One subcluster has pglH while the other has the pglH2 variant allele |
759430 |
| 2.4.1.B69 | malfunction |
pgl genotype and glycosylation phenotype in meningococcal isolates and the changes occurring during short-term asymptomatic carriage. Immunoblotting with glycan-specific antibodies is used to investigate the protein glycosylation phenotype, all major pgl locus polymorphisms identified in Neisseria meningitidis to date, with the variable presence of pglG and pglH, both in combination with either pglB or pglB2. Polymorphisms exist at the gene level described for pglH and pglH2, where only one nonsynonymous mutation is accountable for the glycoform switch from Glc to GlcNAc |
759430 |
| 2.4.1.B69 | malfunction |
pgl genotype and glycosylation phenotype in meningococcal isolates and the changes occurring during short-term asymptomatic carriage. Immunoblotting with glycan-specific antibodies is used to investigate the protein glycosylation phenotype, all major pgl locus polymorphisms identified in Neisseria meningitidis to date, with the variable presence of pglG and pglH, both in combination with either pglB or pglB2. Polymorphisms in gene pglG, e.g. blocks of nucleotides 3' to the poly(C) region are changed, genotype-phenotype relations, overview |
759430 |
| 2.4.1.B69 | more |
more than 30 different glycoforms can be synthesized by combinations of glycosyltransferases and the O-acetylase within neisserial species |
759430 |
| 2.4.1.B69 | physiological function |
a null mutation in PglH leads to the expression of a diNAcBac monosaccharide glycoform. PglH protein participates in the synthesis of Und-PP-diNAcBac-Glc (i.e. undecaprenyl diphosphate-4-glyceramido-2-acetamido-2,4,6-trideoxy-alpha-D-hexose) similarly to its gonococcal and meningococcal orthologues |
736369 |
| 2.4.1.B69 | physiological function |
allelic polymorphisms in the pglH gene lead to neisserial glycoform diversification |
736831 |
| 2.4.1.B69 | physiological function |
PglG is characterized as a glycosyltransferase that elaborates the undecaprenyl diphosphate-linked disaccharide in Neisseria elongata subsp. glycolytica with di-N-acetyl hexuronic acid, but no PglG activity has been detected in pathogenic Neisseria species |
759430 |
| 2.4.1.B69 | physiological function |
PglH is a glucosyltransferase that acts on both N,N'-diacetylbacillosamine (diNAcBac) and glyceramido-acetamido trideoxyhexose (GATDH) to generate glucose (Glc)-containing disaccharides. Although half of the isolates had pglH on, only five of these had pDAb2 reactivity. Some isolates have no competing glycosyltransferases for PglH and are therefore expected to synthesize PglH disaccharide |
759430 |
