TY - JOUR
T1 - Conservation of the lipooligosaccharide synthesis locus lgt among strains of Neisseria gonorrhoeae
T2 - requirement for lgtE in synthesis of the 2C7 epitope and of the β chain of strain 15253
AU - Erwin, Alice L.
AU - Haynes, Paul A.
AU - Rice, Peter A.
AU - Gotschlich, Emil C.
PY - 1996/10/1
Y1 - 1996/10/1
N2 - The present study was undertaken to examine the extent to which the lgt locus varies among strains of gonococci. This locus encodes five glycosyl transferases involved in the synthesis of the lipooligosaccharide (LOS) of Neisseria gonorrhoea. We examined seven gonococcal strains and found that the structure of the lgt locus is conversed among six of these strains. The locus is strikingly altered in strain 15253. This is one of the few strains where extensive structural analysis of its LOS is available, and therefore, we defined the altered lgt locus and focused on the reactivity of mAB 2C7. We found that strain 15253 contains only two lgt genes, lgtA and lgtE. As in F62, lgtA encodes a GlcNAc transferase and is subject to phase variation. In addition, by analysis of deletion mutants, we found that lgtE, which encodes a galactosyl transferase that is required for elongating the α-chain, is also necessary for completing the β chain.
AB - The present study was undertaken to examine the extent to which the lgt locus varies among strains of gonococci. This locus encodes five glycosyl transferases involved in the synthesis of the lipooligosaccharide (LOS) of Neisseria gonorrhoea. We examined seven gonococcal strains and found that the structure of the lgt locus is conversed among six of these strains. The locus is strikingly altered in strain 15253. This is one of the few strains where extensive structural analysis of its LOS is available, and therefore, we defined the altered lgt locus and focused on the reactivity of mAB 2C7. We found that strain 15253 contains only two lgt genes, lgtA and lgtE. As in F62, lgtA encodes a GlcNAc transferase and is subject to phase variation. In addition, by analysis of deletion mutants, we found that lgtE, which encodes a galactosyl transferase that is required for elongating the α-chain, is also necessary for completing the β chain.
UR - http://www.scopus.com/inward/record.url?scp=0029961892&partnerID=8YFLogxK
U2 - 10.1084/jem.184.4.1233
DO - 10.1084/jem.184.4.1233
M3 - Article
C2 - 8879194
AN - SCOPUS:0029961892
SN - 0022-1007
VL - 184
SP - 1233
EP - 1241
JO - Journal of Experimental Medicine
JF - Journal of Experimental Medicine
IS - 4
ER -