Hill D E, Fetterer R H, Urban J F
U.S. Department of Agriculture, Agricultural Research Service, Beltsville, Maryland 20705.
Exp Parasitol. 1991 Oct;73(3):376-83. doi: 10.1016/0014-4894(91)90110-i.
A glycosylated component with affinity for wheat germ agglutinin (specific binding to n-acetyl-D-glucosamine monomers and oligomers) and weak affinity for poke weed mitogen (specific binding to n-acetyl-D-glucosamine oligomers) was detected temporally on the surface of Ascaris suum larvae developing in vitro and on in vivo-derived larvae. The component was identified on the surface of in vitro-derived late second stage larvae, on all late third stage larvae (derived from pig lung), and all fourth stage larvae (obtained from pig intestines and from in vitro culture) of A. suum. None of the newly hatched first molt, L2, or early L3 bound any of the lectins tested. The component exhibited no affinity for concanavalin A (specific binding to alpha-D-mannosyl and alpha-D-glucosyl residues) or Dolichos biflorus lectin (specific binding to n-acetyl-D-galactosamine). A component with similar lectin binding specificities had previously been found on the cuticle of adult A. suum.
在体外培养发育的猪蛔虫幼虫表面以及体内来源的幼虫表面,暂时检测到一种糖基化成分,该成分对麦胚凝集素具有亲和力(特异性结合N-乙酰-D-葡萄糖胺单体和低聚物),对商陆有丝分裂原具有弱亲和力(特异性结合N-乙酰-D-葡萄糖胺低聚物)。在体外培养的猪蛔虫晚期第二阶段幼虫表面、所有晚期第三阶段幼虫(源自猪肺)以及所有第四阶段幼虫(从猪肠道和体外培养获得)的表面均鉴定出该成分。新孵化的第一龄幼虫、第二阶段幼虫或早期第三阶段幼虫均未与所测试的任何凝集素结合。该成分对刀豆球蛋白A(特异性结合α-D-甘露糖基和α-D-葡萄糖基残基)或双花扁豆凝集素(特异性结合N-乙酰-D-半乳糖胺)无亲和力。之前在成年猪蛔虫的角质层上发现了一种具有类似凝集素结合特异性的成分。