Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules

نویسندگان

  • E Nössner
  • P Parham
چکیده

Previous studies have shown that immature mouse class I molecules transiently associate with a resident endoplasmic reticulum protein of 88 kD that has been proposed to act as a chaperone for class I assembly. Subsequently, this protein was demonstrated to be identical to calnexin and to associate with immature forms of the T cell receptor complex, immunoglobulin, and human class I HLA heavy chains. In this paper we define further the interaction of human class I HLA heavy chains with chaperone proteins and find key differences with the complexes observed in the mouse system. First, calnexin and immunoglobulin binding protein (BiP) both associate with immature HLA class I heavy chains. The two chaperones are not found within the same molecular complex, suggesting that calnexin and BiP do not interact simultaneously with the same HLA class I heavy chain. Second, only free HLA class I heavy chains, and not beta 2-microglobulin (beta 2m)-associated heavy chains are found associated with the chaperones. Indeed, addition of free beta 2m in vitro induces dissociation of chaperone-class I HLA heavy chain complexes. The kinetics for dissociation of the class I HLA heavy chain-chaperone complexes and for formation of the class I HLA heavy chain-beta 2m complex display a reciprocity that suggests the interactions with chaperone and beta 2m are mutually exclusive. Mouse class I heavy chains expressed in human cells exhibit the mouse pattern of interaction with human chaperones and human beta 2m and not the human pattern, showing the difference in behavior is purely a function of the class I heavy chain sequence.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Comparative Genomics of Natural Killer Cell Receptor Gene Clusters

Many receptors on natural killer (NK) cells recognize major histocompatibility complex class I molecules in order to monitor unhealthy tissues, such as cells infected with viruses, and some tumors. Genes encoding families of NK receptors and related sequences are organized into two main clusters in humans: the natural killer complex on Chromosome 12p13.1, which encodes C-type lectin molecules, ...

متن کامل

Identification of Mycobacterium tuberculosis CTL Epitopes Restricted by HLA-A*0201 in HHD Mice

CD8+ T cells are thought to play an important role in protective immunity to tuberculosis. The major histocompatibility complex class I subtype HLA-A*0201 is one of the most prevalent class I alleles, with a frequency of over 30% in most populations. HLA-A*0201 transgenic, H-2Db/mouse beta2-microglobulin double-knockout mice (HHD) which express human HLA-A*0201 but no mouse class I, was shown t...

متن کامل

Isolation and purification of HLA-DR antigen from Daudi cell line by immunoaffinity chromatography

Introduction: The major histocompatibility complex (MHC) is a group of cell surface proteins that are essential for recognizing foreign molecules in human and other mammals. The physiologic function of MHC molecules is the presentation of peptides to T cells. In this study, we evaluated the purification of a class II MHC molecule (HLA-DR) from a human Burkitt′s lymphoma cell line; Daudi...

متن کامل

Identification and characterization of major histocompatibility complex class IIB alleles from three species of European ranid frogs

Immune genes of the major histocompatibility complex (MHC) are among the most polymorphic genes in the vertebrate genome. Due to their polymorphic nature, they are often used to assess the adaptive genetic variability of natural populations. This study describes the first molecular characterization of 13 partial MHC class IIB sequences from three European ranid frogs.  The utility of previously...

متن کامل

Distinct patterns of folding and interactions with calnexin and calreticulin in human class I MHC proteins with altered N-glycosylation.

Calnexin is a lectin-like chaperone that binds to class I MHC molecules soon after their synthesis, retaining unassembled heavy chains and also assisting their folding. Following association with beta2-microglobulin (beta2m) in the endoplasmic reticulum, a large proportion of human class I molecules release from calnexin, whereas mouse class I molecules do not. We asked whether addition of a se...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of Experimental Medicine

دوره 181  شماره 

صفحات  -

تاریخ انتشار 1995