Mandrell R E, Griffiss J M, Smith H, Cole J A
Centre for Immunochemistry, Veterans Administration Medical Center/113A, San Francisco, CA 94121.
Microb Pathog. 1993 Apr;14(4):315-27. doi: 10.1006/mpat.1993.1031.
Sialyltransferase activity has been detected in Triton X100 extracts of all examined strains of pathogenic Neisseria as well as in 17 out of 18 Neisseria lactamica isolates. The enzyme was detected both in strains able to synthesize the 4.5 kDa lipooligosaccharide (LOS) component known to be sialylated in vivo and in vitro by cytidine 5'-monophospho-N-acetylneuraminic acid, and in some strains which lack this component. Exogenous 4.5 kDa+ LOS was required to detect the sialyltransferase activity in strains which lacked the LOS component. Sialyltransferase activity in a serogroup A, L11 (4.5 kDa-) meningococcal strain sialylated exogenous purified LOS from gonococci. The meningococcal serogroup B and C strain sialyltransferases active with LOS acceptors appeared to be distinct from the sialyltransferase required for the synthesis of the meningococcal polysialic acid capsule.
在所有检测的致病性奈瑟菌菌株的Triton X100提取物中以及18株乳酸奈瑟菌分离株中的17株中检测到了唾液酸转移酶活性。该酶在能够合成已知在体内和体外被胞苷5'-单磷酸-N-乙酰神经氨酸唾液酸化的4.5 kDa脂寡糖（LOS）成分的菌株中以及在一些缺乏该成分的菌株中均被检测到。对于缺乏LOS成分的菌株，需要外源性4.5 kDa + LOS来检测唾液酸转移酶活性。A血清群、L11（4.5 kDa -）脑膜炎球菌菌株中的唾液酸转移酶活性使来自淋球菌的外源性纯化LOS唾液酸化。对LOS受体有活性的B和C血清群脑膜炎球菌菌株唾液酸转移酶似乎与合成脑膜炎球菌多唾液酸荚膜所需的唾液酸转移酶不同。
