Hmdb loader
Identification
HMDB Protein ID HMDBP14359
Secondary Accession Numbers None
Name N-acetyllactosaminide alpha-2,3-sialyltransferase
Synonyms
  1. CMP-N-acetylneuraminate:beta-galactoside alpha-2,3-sialyltransferase
  2. Lipooligosaccharide sialyltransferase
  3. CMP-Neu5Ac:beta-galactoside alpha-2,3-sialyltransferase
  4. LOS sialyltransferase
Gene Name LST
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Catalyzes the transfer of sialic acid from the substrate CMP-N-acetylneuraminate to the terminal galactose residue of the lacto-N-neotetraose branch of surface lipooligosaccharide (LOS), forming an alpha-2,3-sialyl linkage. Thus, functions in the sialylation of LOS, which plays a role in the evasion of the host immune response by protecting N.meningitidis from complement-mediated serum killing and from phagocytic killing by neutrophils. In vitro, can use a number of different synthetic acceptors with lactose or galactose as the saccharide portion, but shows a strong preference for the N-acetyllactosamine containing acceptor.
Pathways
  • lipooligosaccharide biosynthesis
Reactions Not Available
GO Classification
Biological Process
lipopolysaccharide biosynthetic process
Cellular Component
cell outer membrane
Molecular Function
N-acetyllactosaminide alpha-2,3-sialyltransferase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 371
Molecular Weight 42610.84
Theoretical pI 8.593
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P72097
UniProtKB/Swiss-Prot Entry Name LST_NEIMB
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Tettelin H, Saunders NJ, Heidelberg J, Jeffries AC, Nelson KE, Eisen JA, Ketchum KA, Hood DW, Peden JF, Dodson RJ, Nelson WC, Gwinn ML, DeBoy R, Peterson JD, Hickey EK, Haft DH, Salzberg SL, White O, Fleischmann RD, Dougherty BA, Mason T, Ciecko A, Parksey DS, Blair E, Cittone H, Clark EB, Cotton MD, Utterback TR, Khouri H, Qin H, Vamathevan J, Gill J, Scarlato V, Masignani V, Pizza M, Grandi G, Sun L, Smith HO, Fraser CM, Moxon ER, Rappuoli R, Venter JC: Complete genome sequence of Neisseria meningitidis serogroup B strain MC58. Science. 2000 Mar 10;287(5459):1809-15. doi: 10.1126/science.287.5459.1809. [PubMed:10710307 ]
  2. Vipond C, Wheeler JX, Jones C, Feavers IM, Suker J: Characterization of the protein content of a meningococcal outer membrane vesicle vaccine by polyacrylamide gel electrophoresis and mass spectrometry. Hum Vaccin. 2005 Mar-Apr;1(2):80-4. doi: 10.4161/hv.1.2.1651. Epub 2005 Mar 2. [PubMed:17038831 ]
  3. Vipond C, Suker J, Jones C, Tang C, Feavers IM, Wheeler JX: Proteomic analysis of a meningococcal outer membrane vesicle vaccine prepared from the group B strain NZ98/254. Proteomics. 2006 Jun;6(11):3400-13. doi: 10.1002/pmic.200500821. [PubMed:16645985 ]
  4. Gilbert M, Watson DC, Cunningham AM, Jennings MP, Young NM, Wakarchuk WW: Cloning of the lipooligosaccharide alpha-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae. J Biol Chem. 1996 Nov 8;271(45):28271-6. doi: 10.1074/jbc.271.45.28271. [PubMed:8910446 ]
  5. Shell DM, Chiles L, Judd RC, Seal S, Rest RF: The Neisseria lipooligosaccharide-specific alpha-2,3-sialyltransferase is a surface-exposed outer membrane protein. Infect Immun. 2002 Jul;70(7):3744-51. doi: 10.1128/IAI.70.7.3744-3751.2002. [PubMed:12065517 ]
  6. Lin LY, Rakic B, Chiu CP, Lameignere E, Wakarchuk WW, Withers SG, Strynadka NC: Structure and mechanism of the lipooligosaccharide sialyltransferase from Neisseria meningitidis. J Biol Chem. 2011 Oct 28;286(43):37237-48. doi: 10.1074/jbc.M111.249920. Epub 2011 Aug 31. [PubMed:21880735 ]