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'T' Domain of LFA-1 in Selective Binding to Ligands ICAM-1 and ICAM-3 R

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'T' Domain of LFA-1 in Selective Binding to Ligands ICAM-1 and ICAM-3 R Involvement of the 'T' Domain of LFA-1 in Selective Binding to Ligands ICAM-1 and ICAM-3 R. Clive Landis,* Alison McDowall,* Claire L. L. Holness,** Amanda J. Littler,* David L. Simmons,* and Nancy Hogg* * Leukocyte Adhesion Laboratory, Imperial Cancer Research Fund, London WC2A 3PX, United Kingdom; and ~Cell Adhesion Laboratory, Imperial Cancer Research Fund, Institute for Molecular Medicine, Oxford OX3 9DU, United Kingdom Abstract. To analyze the binding requirements of ent on ICAM-3 but not ICAM-1. The epitopes of LFA-1 for its two most homologous ligands, ICAM-1 mAbs YTH81.5 and 122.2A5 were shown to map to and ICAM-3, we compared the effects of various LFA-1 the I domain of the LFA-1 o~ subunit. A third I domain activation regimes and a panel of anti-LFA-1 mAbs mAb, MEM-83, has been previously reported to uni- in T cell binding assays to ICAM-1 or ICAM-3 coated quely activate LFA-1 to bind ICAM-1 (Landis, R. C., on plastic. These studies demonstrated that T cell R. I. Bennett, and N. Hogg. 1993. J. Cell Biol. binding to ICAM-3 was inducible both from the ex- 120:1519-1527). We now show that mAb MEM-83 is terior of the cell by Mn 2+ and from the interior by an not able to stimulate binding of T cells to ICAM-3 agonist of the "inside-out" signaling pathway. T cells over a wide concentration range. Failure to induce bound both ICAM ligands with comparable avidity. A ICAM-3 binding by mAb MEM-83 was not due to a screen of 29 anti-LFA-1 mAbs led to the identification blockade of the ICAM-3 binding site on LFA-1. This of two mAbs specific for the c~ subunit of LFA-1 study has demonstrated that two sets of functionally which selectively blocked adhesion of T cells to distinct mAbs recognizing epitopes in the I domain of ICAM-3 but not ICAM-1. These two mAbs, YTH81.5 LFA-1 are able to exert differential effects on the bind- and 122.2A5, exhibited identical blocking properties ing of LFA-1 to its ligands ICAM-1, and ICAM-3. in a more defined adhesion assay using LFA-1 trans- These results suggest for the first time that LFA-1 is fected COS cells binding to immobilized ligand. Block- capable of binding these two highly homologous ing was not due to a steric interference between anti- ligands in a selective manner and that the I domain LFA-1 mAbs and N-linked carbohydrate residues pres- plays a role in this process. HE integrin lymphocyte function-associated antigen cal integfin composed of a unique ct subunit (CDlla) (Larson (LFA)~-I mediates adhesion events between leuko- et al., 1989) and a common 132 subunit (CD18) (Kishimoto T cytes and a variety of other cell types which express et al., 1987; Law et al., 1987). The c~ subunit contains a one or more of its ligands, namely interceUular adhesion 197-amino acid "inserted" (or "I') domain located between molecule (ICAM)-I (Simmons et al., 1988; Staunton et al., repeated domains 2 and 3. A closely related I domain is pres- 1988), ICAM-2 (Staunton et al., 1989), and ICAM-3 (Faw- ent in the other two/32-type integrins, Mac-1 and p150,95, cett et al., 1992; Vazeux et al., 1992; de Fougerolles et al,, and also two members of the/3~ integrins, very late antigen 1993). The ICAM ligands are members of the immunoglob- (VLA)-I and VLA-2 (Corhi et al., 1987, 1988; Ignatius et ulin superfamily (IgSF), with ICAM-1 and ICAM-3 display- al., 1990; Takada and Hemler, 1989). Comparisons of the ing particular similarity. Both are composed of five extracel- intron/exon boundaries of p150,95 with the platelet integrin lular C2-1ike Ig domains and exhibit ~50% amino acid GPllbllla suggest that the I domain has been inserted as an identity rising to 77 % in the second domain. LFA-1 is a typi- evolutionarily conserved unit into the basic integrin struc- ture (Corbi et al., 1990; Heidenreich et al., 1990). Similar Address all correspondence to Dr. Nancy Hogg, Leukocyte Adhesion Labo- domains are present in a number of unrelated proteins and ratory, Imperial Cancer Research Fund, London WC2A 3PX, United the integrin I domains are now recognized as belonging to Kingdom. a larger family of so-called type "A" domain proteins (for re- 1. Abbreviations used in this paper: APC, antigen-presenting cells; ICAM, view see Colomhatti and Bonaldo, 1991). intercellular adhesion molecule; IgSE immunoglobulin superfamily; LFA, LFA-1 mediates leukocyte adhesion events at diverse lymphocyte function-associated antigen; LIB, ligand-induced binding; stages of the immune response, including adhesion to en- PdBu, phorbol dibutyrate; VLA, very late antigen. dothelium and extravasation into inflamed tissues, priming © The Rockefeller University Press, 0021-9525/94/07/529/9 $2.00 The Journal of Cell Biology,Volume 126, Number2, July 1994 529-537 529 of T cells by antigen presenting cells (APCs) and killing of lax domains fused to a human IgG1 Fc fragment (ICAM-Fcs) have been pre- viously described (Fawcett et al., 1992). Each preparation of protein target cells by effector T cells (for review see Harvey et al., A-Sepharose purified ICAM-Fc was checked for purity by SDS-PAGE anal- 1993). The details of which ICAM ligand is used at each of ysis and found to migrate as a single band under reducing conditions of 70 these steps is still unclear, but it is currently thought that kD in the case of ICAM-1 and a diffuse band of between 75-80 kD in the ICAMs-1 and -2 are principally required for leukocyte adhe- case of ICAM-3. ICAM-3-Fc was degiycosylated at 100 #g/mi in buffer con- sion to endothelium, whereas ICAMs-1 and -3 are involved raining 20 mM phosphate, pH 8.0 plus 25 mM EDTA by sequential incuba- tions for 20 and 16 h at 37°C in the presence of 4 and 2 U/ml N-Olycosidase in formation of APC:T cell couples. During the APC:T cell F (Boehringer-Mannheim, UK). For T cell adh~ion assays, ICAM-Fcs interaction ICAM-1 appears to be the favored ligand on were added at 500 ng/well in PBS to Immulon 1 96-well plates (Dynatech memory T cells whereas ICAM-3, which is expressed at Laboratories Inc., Chantilly, VA). For LFA-1/COS cell assays, ICAM-Fcs higher levels on resting T cells, may be initially favored dur- were added at 500 ng/well to Immulon 3 plates precoated with 1 #g/well goat-anti-human-Fc Ig (Sigma Chemical Company Ltd., Dorset, U.K.). ing early stages of primary antigenic responses (de Fou- Plates were coated overnight at 40C and non-specific sites were blocked be- gerolles and Springer, 1992). fore the adhesion assay with 2.5% BSA (Fraction V, Sigma) in PBS for 2 h LFA-1 is not constitutively avid for ICAM-1 (Dustin and at room temperature. All ICAM-Fc constructs were coated to plates at Springer, 1989; van Kooyk et al., 1989) but rapidly acquires saturating levels, as determined by ELISA and T cell binding assays. high avidity binding in response to one of three basic types of signals: (1) agonists that trigger a so-called "inside-out" Monoclonal Antibodies signal in leukocytes, which include phorbol esters or mAbs Anti-LFA-1 ~ subunit mAbs MEM-83 and MEM-94 were generously against other surface receptors, such as CD3, CD2, and provided by Dr. V. Horejsi (Prague, Czech Republic), mAb 122.2A5 by Dr. CD31 (for review see Pardi et al., 1992); (2) changes in the R. Vilella (Barcelona, Spain) and mAb YTH81.5 by Serotec (Oxford, U.K.) extracellular concentrations of the divalent cations Mg2+, (Bazil and Horejsi, 1990; Schmidt, 1989). Anti-ICAM-1 mAb RR1/1 was a gift from Dr. R. Rothlein (Ridgefleld, CT) (Rothlein et al., 1986). The Mn2+, and Ca2+ (Dransfield et al., 1992; Dranstield and remaining mAbs, obtained from Dr. Reinhold Schmidt, were from the Leu- Hogg, 1989); and (3) special "activating" anti-LFA-1 mAbs kocyte Typing Workshop IV (Schmidt, 1989) and included the anti-CDlla which directly induce the ligand-binding conformation on mAbs MHM24, 122.2A5, MEM-95, MEM-30, MEM-25, 2F12, F110.22, the receptor (Andrew et al., 1993; Landis et al., 1993; GRS3, I-roll, MI0, 0501, 25.3.1, 459, YTH 81.5, 1524, TMD3-1, CC5 liT/, Robinson et al., 1992; Keizer et al., 1988). The activation and the anti-CD18 mAbs H-52, MHM23, TS1/18, M232, IC11, CLB-54, IB- 4, YFC 51.1, YFC 118.3, and GRF1. Purified anti-CDlla mAbs MEM-83, epitope for one of these mAbs, MEM-83, has been mapped 38 and YTH81.5 were used in T cell adhesion assays at final concentrations and shown to localize to the I domain, thereby suggesting a of 2-5 #g/ml and in immuno-precipitation assays at 30 #g/ml. mAb regulatory role for this domain in LFA-1 activation. Support 122.2A5 was used as ascitic fluid diluted 1:300 in T cell adhesion assays for such a role has been provided by the finding that a novel and at 1:50 in immunoprecipitatiun assays. Purified anti-ICAM-1 .mAb RRI/1 was used in T cell binding assays at 10 #g/ml and the imrmmoprecipi- Mac-1 "activation-reporter" epitope is also located in the I tation negative control CD8 mAb 14 was used at 30/~g/ml.
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