Kinetics and Energetics of Specific Intermolecular Interactions

Oss, Carel J. van

doi:10.1002/(sici)1099-1352(199709/10)10:5<203::aid-jmr366>3.0.co;2-z

Cited by 43 publications

(25 citation statements)

References 45 publications

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“…Several examples of inhibition of binding of a ligand to its receptor by a MAb binding to a closely juxtaposed molecule have been reported in the literature (21,23,25,36). Our finding that bovine CD18 mediates Lkt-induced lysis is further supported by a recent study from the same laboratory (14).…”

Section: Discussionmentioning

confidence: 99%

Bovine CD18 Is Necessary and Sufficient To Mediate Mannheimia ( Pasteurella ) haemolytica Leukotoxin-Induced Cytolysis

Deshpande

Ambagala

et al. 2002

Infect Immun

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Leukotoxin (Lkt) secreted by Mannheimia (Pasteurella) haemolytica is an RTX toxin which is specific for ruminant leukocytes. Lkt binds to ␤ 2 integrins on the surface of bovine leukocytes. ␤ 2 integrins have a common ␤ subunit, CD18, that associates with three distinct ␣ chains, CD11a, CD11b, and CD11c, to give rise to three different ␤ 2 integrins, CD11a/CD18 (LFA-1), CD11b/CD18 (Mac-1), and CD11c/CD18 (CR4), respectively. Our earlier studies revealed that Lkt binds to all three ␤ 2 integrins, suggesting that the common ␤ subunit, CD18, may be the receptor for Lkt. In order to unequivocally elucidate the role of bovine CD18 as a receptor for Lkt, a murine cell line nonsusceptible to Lkt (P815) was transfected with cDNA for bovine CD18. One of the transfectants, 2B2, stably expressed bovine CD18 on the cell surface. The 2B2 transfectant was effectively lysed by Lkt in a concentration-dependent manner, whereas the P815 parent cells were not. Immunoprecipitation of cell surface proteins of 2B2 with monoclonal antibodies specific for bovine CD18 or murine CD11a suggested that bovine CD18 was expressed on the cell surface of 2B2 as a heterodimer with murine CD11a. Expression of bovine CD18 and the Lkt-induced cytotoxicity of 2B2 cells were compared with those of bovine polymorphonuclear neutrophils and lymphocytes. There was a strong correlation between cell surface expression of bovine CD18 and percent cytotoxicity induced by Lkt. These results indicate that bovine CD18 is necessary and sufficient to mediate Lkt-induced cytolysis of target cells.Mannheimia (Pasteurella) haemolytica serotype 1 is the major bacterial pathogen of bovine pneumonic pasteurellosis, an acute fibrinous pleuropneumonia, which causes extensive economic losses to the cattle industry in North America and other parts of the world (4). M. haemolytica A1 is commonly found in the tonsillar crypts and the upper respiratory tracts of healthy cattle (9). In conjunction with active viral infection and stress factors, M. haemolytica migrates to the lungs, where it multiplies rapidly (7,26). M. haemolytica produces several virulence factors, of which the extracellular leukotoxin (Lkt) is considered the most important one responsible for leukocyte damage in the lung (3, 27). Lkt-induced neutrophil lysis and degranulation have been implicated as the primary causes of the acute inflammation characteristic of pneumonic pasteurellosis (31).Leukotoxin (Lkt) is a 102-kDa glycoprotein which is produced during the logarithmic phase of bacterial growth in vitro (2, 28). Lkt belongs to the family of RTX (repeats in toxins) toxins and shares extensive homology with the exotoxins produced by other gram-negative bacteria such as Escherichia coli (33), Actinobacillus pleuropneumoniae (8), and Actinobacillus actinomycetemcomitans (17). Despite the extensive homology shared by the RTX family, there is a marked dichotomy among the members of the family with respect to target cell specificity. The toxins secreted by E. coli and A. pleuropneumoniae are lytic to erythrocyte...

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Section: Discussionmentioning

confidence: 99%

Bovine CD18 Is Necessary and Sufficient To Mediate Mannheimia ( Pasteurella ) haemolytica Leukotoxin-Induced Cytolysis

Deshpande

Ambagala

et al. 2002

Infect Immun

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“…The net balance between the energy versus distance functions of the aspecific (macroscopic) repulsion that usually prevails between antigen and antibody molecules in aqueous media vis-à -vis the specific (microscopic) attraction between the epitope and paratope of the antigen and the antibody, respectively, determines their propensity for complex formation (15). Rearrangement of solvent water molecules accompanying macromolecular complexation events is believed to be largely responsible for the observed nonlinear thermodynamic phenomena (16).…”

mentioning

confidence: 99%

Thermodynamic Analyses Reveal Role of Water Release in Epitope Recognition by a Monoclonal Antibody against the Human Guanylyl Cyclase C Receptor

Swaminathan¹,

Nandi²,

Visweswariah³

et al. 1999

Journal of Biological Chemistry

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The thermodynamics of a monoclonal antibody (mAb)-peptide interaction have been characterized by isothermal titration microcalorimetry. GCC:B10 mAb, generated against human guanylyl cyclase C, a membraneassociated receptor and a potential marker for metastatic colon cancer, recognizes the cognate peptide epitope HIPPENIFPLE and its two contiguous mimotopes, HIPPEN and ENIFPLE, specifically and reversibly. The exothermic binding reactions between 6.4 and 42°C are driven by dominant favorable enthalpic contributions between 20 and 42°C, with a large negative heat capacity (⌬C p ) of ؊421 ؎ 27 cal mol ؊1 K ؊1 . The unfavorable negative value of entropy (⌬S b 0 ) at 25°C, an unusual feature among protein-protein interactions, becomes a positive one below an inversion temperature of 20.5°C. Enthalpy-entropy compensation due to solvent reorganization accounts for an essentially unchanged free energy of interaction (⌬⌬G b 0 Х 0). The role of water molecules in the recognition process was tested by coupling an osmotic stress technique with isothermal titration microcalorimetry. The results provide direct and compelling evidence that GCC:B10 mAb recognizes the peptides HIPPENIFPLE, HIPPEN, and ENIFPLE differentially, with a concomitant release of variable and nonadditive numbers of water molecules (15, 7, and 3, respectively) from the vicinity of the binding site.Immune system recognition of ligands involves the formation of a multitude of specific intermolecular interactions between the components of the host and the foreign body (1-7). Atomic level investigations on antigen-antibody complex formation reveal that, although charged and polar side chains can be critical in binding, notably important contributions originate from hydrophobic side chains just as they do in other protein-protein complexes (1, 6, 8 -11). Solution state studies of the binding of two different proteins to the same antibody, for example, have shown that, in certain cases, the free energy of binding may arise from the accumulation of many interactions of varying strength over the entire protein-protein interface (12). Thus, the perception as propounded by crystal structural results that protein-protein recognition is mediated by only a few strong interactions may not be a general feature (13). Complications also arise from the observation that a majority of direct contacts in the antigen-antibody complex may be energetically neutral (14). This highlights the need for a complete characterization of binding energetics of antigen-antibody interactions as a prelude to understanding the underlying structural basis of the molecular recognition process.The net balance between the energy versus distance functions of the aspecific (macroscopic) repulsion that usually prevails between antigen and antibody molecules in aqueous media vis-à -vis the specific (microscopic) attraction between the epitope and paratope of the antigen and the antibody, respectively, determines their propensity for complex formation (15). Rearrangement of solvent water molecules acc...

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“…It is necessary to better understand the complex interactions of latex particles in a given carrier phase versus channel wall characteristics. Irreversible as well as reversible particle trapping may be discussed in the future using guidelines given by van Oss in terms of sorption energies [26,27]. In our experience it appears that elution recovery can vary from 40% to 95% depending on FFF operating conditions and the type of sample used.…”

Section: Particle Trappingmentioning

confidence: 79%

Fast “hyperlayer” separation development in sedimentation field flow fractionation☆

Kassab

Cardot

Zahoransky

et al. 2005

Journal of Chromatography B

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Kinetics and Energetics of Specific Intermolecular Interactions

Cited by 43 publications

References 45 publications

Bovine CD18 Is Necessary and Sufficient To Mediate Mannheimia ( Pasteurella ) haemolytica Leukotoxin-Induced Cytolysis

Bovine CD18 Is Necessary and Sufficient To Mediate Mannheimia ( Pasteurella ) haemolytica Leukotoxin-Induced Cytolysis

Thermodynamic Analyses Reveal Role of Water Release in Epitope Recognition by a Monoclonal Antibody against the Human Guanylyl Cyclase C Receptor

Fast “hyperlayer” separation development in sedimentation field flow fractionation☆

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