Molecular characterization of the murine cytotoxic T-cell membrane glycoprotein Ly-3 (CD8).

Panaccio, Michael; Gillespie, Matthew T.; Walker, Ian D.; Kirszbaum, L.; Sharpe, Jennifer A.; Tobias, G H; McKenzie, Ian F. C.; Deacon, Nicholas J.

doi:10.1073/pnas.84.19.6874

Cited by 23 publications

(13 citation statements)

References 37 publications

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“…Antibodies to the mouse CD8 molecules (also known as Ly-2,3) have been shown to precipitate from thymocytes three chains of [35][36][37][38] kDa (a), [30][31][32][33][34] In order to explore the functional role of the Ly-2,3 complex, we have undertaken a series of gene transfer experiments and recently shown that the Ly-3 subunit is not required for Ly-2 to efficiently function in class I MHC recognition [lo]. In order to obtain additional information concerning the possible structure-function relationships existing between the Ly-2 and Ly-3 subunits, we have now isolated and expressed by transfection one Ly-3 cosmid clone.…”

Section: Introductionmentioning

confidence: 99%

Gene transfer of the ly‐3 chain gene of the mouse cd8 molecular complex: co‐transfer with the ly‐2 polypeptide gene results in detectable cell surface expression of the ly‐3 antigenic determinants

et al. 1988

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The CD8 molecule is a glycoprotein expressed on a subset of mature T lymphocytes. It has been postulated to be a receptor for class I major histocompatibility complex molecules. In the mouse, CD8 is a heterodimer composed of Ly-2 and Ly-3 chains. We have isolated and analyzed cDNA and cosmid clones corresponding to the Ly-3 subunit. One of the isolated, cosmid clones was subsequently transfected, alone or in combination with the Ly-2 gene, into mouse Ltk- cells. Analysis of the Ly-2,3 molecules expressed at the surface of the double transfectants indicated that they are serologically and biochemically indistinguishable from their normal counterparts expressed on lymphoid cells. Ltk- cells transfected with the Ly-2 gene alone were shown to react with a subset of anti-CD8 monoclonal antibodies whereas Ly-3 transfectants did not stain with any of the anti-Ly-3 antibodies employed in this study. Since at least one of these antibodies (53-5.8) has been previously shown to recognize an epitope which is retained on the Ly-3 subunit after dissociation of the heterodimeric Ly-2,3 complex, these observations suggest that the expression of the Ly-2 polypeptide is required to permit the detectable cell surface expression of the antigenic determinants carried by the Ly-3 subunit.

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Section: Introductionmentioning

confidence: 99%

Gene transfer of the ly‐3 chain gene of the mouse cd8 molecular complex: co‐transfer with the ly‐2 polypeptide gene results in detectable cell surface expression of the ly‐3 antigenic determinants

et al. 1988

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“…28). CD8␣-and ␤-chains have two and one N-linked glycosylation sites, respectively, in the Ig-like domains where they share Ͻ20% identity in their amino acid sequences (12)(13)(14)(15)26). The CD8␤ stalk region is 10 -13 aa shorter than the CD8␣ stalk and is highly glycosylated with O-linked carbohydrates.…”

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Stalk Region of β-Chain Enhances the Coreceptor Function of CD8

Wong

Wang

Witte

et al. 2003

The Journal of Immunology

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CD8 glycoproteins are expressed as either αα homodimers or αβ heterodimers on the surface of T cells. CD8αβ is a more efficient coreceptor than the CD8αα for peptide Ag recognition by TCR. Each CD8 subunit is composed of four structural domains, namely, Ig-like domain, stalk region, transmembrane region, and cytoplasmic domain. In an attempt to understand why CD8αβ is a better coreceptor than CD8αα, we engineered, expressed, and functionally tested a chimeric CD8α protein whose stalk region is replaced with that of CD8β. We found that the β stalk region enhances the coreceptor function of chimeric CD8αα to a level similar to that of CD8αβ. Surprisingly, the β stalk region also restored functional activity to an inactive CD8α variant, carrying an Ala mutation at Arg8 (R8A), to a level similar to that of wild-type CD8αβ. Using the R8A variant of CD8α, a panel of anti-CD8α Abs, and three MHC class I (MHCI) variants differing in key residues known to be involved in CD8α interaction, we show that the introduction of the CD8β stalk leads to a different topology of the CD8α-MHCI complex without altering the overall structure of the Ig-like domain of CD8α or causing the MHCI to employ different residues to interact with the CD8α Ig domain. Our results show that the stalk region of CD8β is capable of fine-tuning the coreceptor function of CD8 proteins as a coreceptor, possibly due to its distinct protein structure, smaller physical size and the unique glycan adducts associated with this region.

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“…We had shown previously that there were two Ly-3 transcripts of approximately 1-3 kb and 2 3 kb in poly(A)+ RNA from thymus and spleen tissue (in 1:1 and 1:01 abundance, respectively [6]). Furthermore, it was evident that the transcripts of the thymoma ITT( I )75NS (Ly-3-1) diftered in size from those of (C57BL/6X BALB/c) FI thymus and spleen (Ly-3 2) (Fig.…”

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confidence: 94%

“…1 b). The largest allotypic fragment of Ly-3 {14 kb) specifically hybridizes with the 750 bp EcoRl fragment of RCCT 136 (6) and hence encodes at least the nine Cterminal amino acids of the Ly-3 protein and the 3' untranslated region of the L3 kb Ly-3 transcript {Fig. lb.…”

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confidence: 99%

“…1087-1092 and 1300-1305 and useof the latter two may result in the 1-3 kb and 1 -4 kb mRNAs, respectively. Since the Ly-3 cDN A sequence data extends for only 1418 bp (6) it is not possible to comment on the exact origin of the 2-2 kb and 2-3 kb forms of the mRNA in terms of alternative polyadenylation, however, as the cDNA sequence of Nakauchi ei al. (7) terminates at a poly(A) tail afterthe second polyadenylation signal and is 1144 bp long it would appear that our cDN A sequence (1418 bp) represents part of the longer (2-2/2-3 kb) transcript.…”

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confidence: 99%

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Murine Ly‐3 restriction fragment length polymorphism and transcript size differences

1989

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Molecular characterization of the murine cytotoxic T-cell membrane glycoprotein Ly-3 (CD8).

Abstract: The

Cited by 23 publications

References 37 publications

Gene transfer of the ly‐3 chain gene of the mouse cd8 molecular complex: co‐transfer with the ly‐2 polypeptide gene results in detectable cell surface expression of the ly‐3 antigenic determinants

Gene transfer of the ly‐3 chain gene of the mouse cd8 molecular complex: co‐transfer with the ly‐2 polypeptide gene results in detectable cell surface expression of the ly‐3 antigenic determinants

Stalk Region of β-Chain Enhances the Coreceptor Function of CD8

Murine Ly‐3 restriction fragment length polymorphism and transcript size differences

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