Zimmermann C R, Johnson S M, Martens G W, White A G, Pappagianis D
Department of Medical Microbiology and Immunology, School of Medicine, University of California, Davis 95616, USA.
Infect Immun. 1996 Dec;64(12):4967-75. doi: 10.1128/iai.64.12.4967-4975.1996.
A chitinase had been isolated from the culture filtrates of Coccidioides immitis endosporulating spherules and from hyphae and shown to be the coccidioidal complement fixation (CF) and immunodiffusion-CF antigen. In the present study, we made use of our previously determined amino-terminal (N-terminal) sequence of the CF-chitinase to design degenerate oligonucleotide primers and to amplify and sequence a PCR product that coded for the N-terminal portion of the CF-chitinase. The PCR product was used as a hybridization probe to screen a developing spherule-(lambda)ZAP cDNA library, and three hybridizing clones were selected. These clones were converted into their pBluescript expression plasmid form in Escherichia coli and induced to express their recombinant proteins. Lysate from only one clone, pCTS 4-2A, yielded an enzymatically functional CF-chitinase and a line of identity with control immunodiffusion-CF-positive antigen. The pCTS 4-2A insert was sequenced and found to contain a deduced open reading frame coding for a 427-amino-acid polypeptide with an approximate molecular weight of 47 kDa. When purified by a chitin adsorption-desorption method, the recombinant protein exhibited virtually identical characteristics to those of the original C. immitis CF-chitinase. Nondenaturing gels of the pCTS 4-2A E. coli lysates and the purified C. immitis and recombinant CF-chitinase revealed proteins that had chitinase activity and similar relative electrophoretic mobilities. The appearance and relative levels of hybridizing RNA from the developing spherules-endospores (SEs) and hyphae correlated with the appearance or presence and level of CF-chitinase enzyme activity found in SEs culture filtrate and in cellular extracts of developing SE and hyphae. Thus, a functional recombinant CF-chitinase antigen was produced in E. coli and was used in serological diagnostic applications. These results also suggest a functional role for this chitinase in SE development and maturation.
已从粗球孢子菌内生孢子球的培养滤液以及菌丝中分离出一种几丁质酶,并证明其为球孢子菌补体结合(CF)及免疫扩散 - CF抗原。在本研究中,我们利用先前测定的CF - 几丁质酶的氨基末端(N末端)序列设计简并寡核苷酸引物,扩增并测序编码CF - 几丁质酶N末端部分的PCR产物。该PCR产物用作杂交探针,筛选正在发育的孢子球 - (λ)ZAP cDNA文库,选择了三个杂交克隆。这些克隆在大肠杆菌中转化为其pBluescript表达质粒形式,并诱导表达其重组蛋白。仅来自一个克隆pCTS 4 - 2A的裂解物产生了具有酶活性的功能性CF - 几丁质酶,并且与对照免疫扩散 - CF阳性抗原具有一条同一性条带。对pCTS 4 - 2A插入片段进行测序,发现其含有一个推导的开放阅读框,编码一个427个氨基酸的多肽,分子量约为47 kDa。当通过几丁质吸附 - 解吸方法纯化时,重组蛋白表现出与原始粗球孢子菌CF - 几丁质酶几乎相同的特性。pCTS 4 - 2A大肠杆菌裂解物以及纯化的粗球孢子菌和重组CF - 几丁质酶的非变性凝胶显示出具有几丁质酶活性且相对电泳迁移率相似的蛋白质。来自正在发育的孢子球 - 内生孢子(SE)和菌丝的杂交RNA的出现和相对水平与在SE培养滤液以及正在发育的SE和菌丝的细胞提取物中发现的CF - 几丁质酶活性的出现、存在和水平相关。因此,在大肠杆菌中产生了功能性重组CF - 几丁质酶抗原,并用于血清学诊断应用。这些结果还表明该几丁质酶在SE发育和成熟中具有功能性作用。