N-Acetylneuraminic acid

N-Acetylneuraminic acid
IUPAC name 5-(acetylamino)-3,5-dideoxy-D-glycero-α-D-galacto-non-2-ulopyranosonic acid
Identifiers
CAS number	131-48-6
PubChem	439197
ChemSpider	392681 Y
MeSH	N-Acetylneuraminic+Acid
Jmol-3D images	Image 1
SMILES OC(=O)[C@@]1(O)C[C@H](O)[C@@H](NC(C)=O)[C@@H](O1)[C@H](O)[C@H](O)CO
InChI InChI=1S/C11H19NO9/c1-4(14)12-7-5(15)2-11(20,10(18)19)21-9(7)8(17)6(16)3-13/h5-9,13,15-17,20H,2-3H2,1H3,(H,12,14)(H,18,19)/t5-,6+,7+,8+,9+,11+/m0/s1 Y Key: SQVRNKJHWKZAKO-YRMXFSIDSA-N Y InChI=1/C11H19NO9/c1-4(14)12-7-5(15)2-11(20,10(18)19)21-9(7)8(17)6(16)3-13/h5-9,13,15-17,20H,2-3H2,1H3,(H,12,14)(H,18,19)/t5-,6+,7+,8+,9+,11+/m0/s1 Key: SQVRNKJHWKZAKO-YRMXFSIDBI
Properties
Molecular formula	C11H19NO9
Molar mass	309.27 g mol−1
Exact mass	309.105981
Appearance	White crystalline powder
Melting point	186°C (decomposes)
Y acid (verify) (what is: Y/N?) Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)
Infobox references

N-Acetylneuraminic acid (Neu5Ac or NANA) is the predominant sialic acid found in mammalian cells.

This negatively charged residue is found in complex glycans on mucins and glycoproteins found at the cell membrane. Neu5Ac residues are also found in glycolipids, such as gangliosides, a crucial component of neuronal membranes found in the brain.

Along with involvement in preventing infections (mucus associated with mucous membranes — mouth, nose, GI, respiratory tract), Neu5Ac acts as a receptor for influenza viruses, allowing attachment to mucous cells via hemagglutinin (an early step in acquiring influenzavirus infection).

Neu5Ac in the biology of bacterial pathogens

Neu5Ac is also important in the biology of a number of pathogenic bacteria ^[1][2] as it can used used either as a nutrient, providing both carbon and nitrogen to the bacterium, or in some pathogens, can be activated and placed on the cell surface.^[1] Bacteria have evolved transporters for Neu5Ac to enable them to capture it from their environment and a number of these have been characterised including the NanT protein from Escherichia coli,^[3] the SiaPQM TRAP transporter from Haemophilus influenze ^[4] and the SatABCD ABC transporter from Haemophilus ducreyi.^[5]

References

1. ^ ^{a b} Severi E, Hood DW, Thomas GH (2007). "Sialic acid utilization by bacterial pathogens". Microbiology 153 (9): 2817–2822. PMID 17768226. 
2. ^ Vimr ER, Kalivoda KA, Deszo EL, Steenbergen SM. (2004). "Diversity of microbial sialic acid metabolism.". Microbiol Mol Biol Rev 68 (1): 132–153. PMID 15007099. 
3. ^ Vimr ER, Troy FA. (1985). "Identification of an inducible catabolic system for sialic acids (nan) in Escherichia coli". J. Bacteriol. 164 (2): 845–853. PMID 3902799. 
4. ^ Severi E, Randle G, Kivlin P, Whitfield K, Young R, Moxon R, Kelly D, Hood D, Thomas GH. (2005). "Sialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP-independent periplasmic transporter". Mol. Microbiol. 58 (4): 1173–1185. doi:10.1111/j.1365-2958.2005.04901.x. PMID 16262798. 
5. ^ Post DM, Mungur R, Gibson BW, Munson RS Jr. (2005). "Identification of a novel sialic acid transporter in Haemophilus ducreyi.". Infect Immun 73 (10): 6727–35. PMID 16177350. 

See also

• Neuraminic acid
• Sialic acid
• N-Glycolylneuraminic acid