Incomplete assembly of IgA2m(2) in Chinese hamster ovary cells

被引：13

作者：

Chintalacharuvu, Koteswara R.

Gurbaxani, Brian

Morrison, Sherie L.

机构：

[1] Univ Calif Los Angeles, Dept Microbiol Immunol & Mol Genet, Los Angeles, CA 90095 USA

[2] Univ Calif Los Angeles, Mol Biol Inst, Los Angeles, CA 90095 USA

来源：

MOLECULAR IMMUNOLOGY | 2007年 / 44卷 / 13期

关键词：

expression in CHO cells; IgA; IgA2m(2); disulfide bond instability;

D O I：

10.1016/j.molimm.2006.12.030

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Myeloma and Chinese hamster ovary (CHO) cells are frequently used for the production of recombinant antibodies. With increasing interest in producing recombinant IgA for protection against infectious agents, it is essential to characterize the IgA produced in these cells. Here we show that while myeloma cells secrete IgA2m(2) predominantly as H2L2, CHO cells secrete H2L and H, in addition to fully assembled H2L2. When the CHO cells also synthesize J chain and secretory component (SC). polymeric IgA and secretory IgA in which SC is disulfide bonded to the polymeric IgA are produced. Blocking cysteines on purified I-A2m(2) protein by alkylating with iodoacetamide stabilizes the disulfide bonds between the H and L chains suggesting that the disulfide bonds between H and L chains are unstable. Taken together our results suggest that the covalent assembly of IgA2m(2) is different in myeloma and CHO cells. (c) 2007 Published by Elsevier Ltd.

引用

页码：3445 / 3452

页数：8

共 33 条

[1] In vitro comparison of the antigen-binding and stability properties of the various molecular forms of IgA antibodies assembled and produced in CHO cells [J].