Expression and function of transplantation antigens with altered or deleted cytoplasmic domains

Zúñiga, Martha C.; Malissen, Bernard; McMillan, Minnie; Brayton, Peter R.; Clark, Stephen S.; Forman, James; Hood, Leroy

doi:10.1016/0092-8674(83)90386-0

Cited by 103 publications

(66 citation statements)

References 26 publications

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“…Rose and Bergmann (22) have obtained evidence that the cytoplasmic domain of VSV G protein plays a critical role in the kinetics of transport, although it is not essential for transport to the plasma membrane. Mutants containing a deletion of the H-2Ld transplantation antigen genes of mice (either missing the majority of the cytoplasmic tail or containing short replacements for the cytoplasmic tail sequence) transported and expressed the antigen on the plasma membrane with the same kinetics as the wild-type antigen (28), indicating that the cytoplasmic tail is not involved in the transport of this protein. We have, however, noted an apparent difference in the pattern of immunofluorescence and immunogold labeling between SNC and SN10 polypeptides, suggesting an inherent difference in the mobility of these gene products.…”

Section: Discussionmentioning

confidence: 99%

Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells.

Jones¹,

Compans²,

Davis³

et al. 1985

Mol. Cell. Biol.

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We have investigated the site of surface expression of the neuraminidase (NA) glycoprotein of influenza A virus, which, in contrast to the hemagglutinin, is bound to membranes by hydrophobic residues near the NH2-terminus. Madin-Darby canine kidney or primary African green monkey kidney cells infected with influenza A/WSN/33 virus and subsequently labeled with monoclonal antibody to the NA and then with a colloidal gold-or ferritin-conjugated second antibody exhibited specific labeling of apical surfaces. Using simian virus 40 late expression vectors, we also studied the surface expression of the complete NA gene (SNC) and a truncated NA gene (SN10) in either primary or a polarized continuous line (MA104) of African green monkey kidney cells. The polypeptides encoded by the cloned NA cDNAs were expressed on the surface of both cell types. Analysis of [3H]mannose-labeled polypeptides from recombinant virus-infected MA104 cells showed that the products of cloned NA cDNA comigrated with glycosylated NA from influenza virus-infected cells. Both the complete and the truncated glycoproteins were found to be preferentially expressed on apical plasma membranes, as detected by immunogold labeling. These results indicate that (i) the NA polypeptide contains structural features capable of directing the transport of the protein to apical cell surfaces and (ii) the first 10 amino-terminal residues of the NA polypeptide are not involved in this process.

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Section: Discussionmentioning

confidence: 99%

Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells.

Jones¹,

Compans²,

Davis³

et al. 1985

Mol. Cell. Biol.

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“…Such studies suggested that the cytoplasmic domains of at least some proteins might constitute signals that facilitate transport to the cell surface. Deletions have also been constructed in regions of cDNA clones which specify the cytoplasmic domains of the Semliki Forest virus E2 glycoprotein (18) or a murine major histocompatibility antigen (H-2L d) (39,65). These mutant glycoproteins are expressed on the cell surface.…”

mentioning

confidence: 99%

Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane.

Puddington¹,

Machamer²,

Rose³

1986

The Journal of Cell Biology

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Abstract. Oligonucleotide-directed mutagenesis was used to construct chimeric cDNAs that encode the extracellular and transmembrane domains of the vesicular stomatitis virus glycoprotein (G) linked to the cytoplasmic domain of either the immunoglobulin u membrane heavy chain, the hemagglutinin glycoprotein of influenza virus, or the small glycoprotein (023) of infectious bronchitis virus. Biochemical analyses and immunofluorescence microscopy demonstrated that these hybrid genes were correctly expressed in eukaryotic cells and that the hybrid proteins were transported to the plasma membrane. The rate of transport to the Golgi complex of G protein with an immunoglobulin # membrane cytoplasmic domain was approximately sixfold slower than G protein with its normal cytoplasmic domain. However, this rate was virtually identical to the rate of transport of ~m heavy chain molecules measured in the B cell line WEHI 231. The rate of transport of G protein with a hemagglutinin cytoplasmic domain was threefold slower than wild type G protein and G protein with a p23 cytoplasmic domain, which were transported at similar rates. The combined results underscore the importance of the amino acid sequence in the cytoplasmic domain for efficient transport of G protein to the cell surface. Also, normal cytoplasmic domains from other transmembrane glycoproteins can substitute for the G protein cytoplasmic domain in transport of G protein to the plasma membrane. The method of constructing precise hybrid proteins described here will be useful in defining functions of specific domains of viral and cellular integral membrane proteins.

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“…Because it is not clear what happens before the cytoplasmic domain, it is difficult to predict which reading frame would be used if the mRNA were translated, but if the proper reading frame was encoded, an additional 43 amino acids would be encoded as a result of A5906. The effect of additional amino acids in the cytoplasmic tail of class II molecules is unknown, but deletion experiments involving cytoplasmic domains of other MHC antigens suggest that it is not needed for many functions (29). Overall, the combined mutations would result in a frameshifted, improperly spliced mRNA which, if translated, would result in a protein resembling a class II a chain for only the first 80 amino acids, unless, as discussed, a proximal alternative splice site was used, shortening the al domain by eight amino acids.…”

Section: Dr -Fda-spl----n-v----tv----i-i--if--g--ksnaaerr-p-dq -Pei-amentioning

confidence: 99%

“…Considering the above mutations in this gene, the abnormally long cytoplasmic tail is least likely to have an effect. It has been shown by exon deletion and shuffling experiments that the cytoplasmic tail is not necessary for class I MHC molecules to function properly in the systems assayed (29).…”

Section: Dr -Fda-spl----n-v----tv----i-i--if--g--ksnaaerr-p-dq -Pei-amentioning

confidence: 99%

Sequence analysis of the human major histocompatibility gene SX alpha.

Boss¹,

Mengler²,

Okada³

et al. 1985

Mol. Cell. Biol.

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The DP subregion of the human major histocompatibility complex contains two closely linked gene pairs, DPa, DPOi and SXa, SX13. The exon-intron organization and the complete DNA sequence of the SXa gene are reported here. There are several mutations within the SXot gene which strongly suggest that it is a pseudogene. These include two frameshift mutations, one in the al domain and the other in the cytoplasmic domain. A 5' splice site mutation at the end of the aLl exon also exists. DNA sequence homology between DPoa and SXot suggests that these genes arose through a gene duplication event.The class II genes of the major histocompatibility complex (MHC) encode cell surface glycoproteins that function in the regulation of the immune response by association with "processed" foreign antigen to provide a recognition unit for helper T cells as well as for class TI-directed cytotoxic T cells. Class II MHC proteins are heterodimers (an a chain of 33 kilodaltons and a 1 chain of 29 kilodaltons [21]) and in humans are found on the surfaces of B cells, macrophages, and activated T cells. In humans the class II genes are located within the HLA-D region of chromosome 6. This region is homologous to the Ia region of chromosome 17 in mice. To date six human a-chain genes and seven 13-chain genes have been cloned as cDNAs or as genomic clones (for reviews see reference 8 and A. J. Korman, J. M. Boss, T: Spies, R. Sorrentino, K. Okada, and J. L. Strominger, Immunol. Rev., in press). The cloning and subsequent sequence analyses of some of these genes have helped organize the genes into three families. The DR region contains one a-and three 13-chain genes (22a); the DQ (formally DC) region contains the DQa and DQ,B genes as well as a homologous pair of DQ-like genes called DXa and DX1 (16a). The DR and DQ families have analogous counterparts in mice, namely, IE and IA, respectively. The third family, DP (formally SB), has been shown to contain four genes which are closely linked, i.e., within 120 kilobases (kb) of DNA (17,20,24

show abstract

Expression and function of transplantation antigens with altered or deleted cytoplasmic domains

Cited by 103 publications

References 26 publications

Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells.

Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells.

Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane.

Sequence analysis of the human major histocompatibility gene SX alpha.

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