Interactions of protein antigens with antibodies.

Davies, David R.; Cohen, Gerald

doi:10.1073/pnas.93.1.7

Cited by 512 publications

(334 citation statements)

References 62 publications

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“…5). This is consistent with the trend that has been observed to date in Ab-Ag complexes (3,29,30). In all the three complexes, the epitope is present in a groove in the Ag-combining site, as has been observed for other Ab-peptide complexes (2,31,32).…”

Section: Ag-ab Interactionssupporting

confidence: 91%

“…Three-dimensional structures of the mAbs and their complexes with the corresponding Ags of diverse origins have provided critical insights regarding humoral immune recognition (1)(2)(3). These studies have contributed immensely toward the understanding of different aspects of an immune response, such as repertoire shift, affinity maturation, idiotype networks, and crossreactivity (4 -8).…”

mentioning

confidence: 99%

“…The Abs PC283, PC282, and PC287 belong to the isotypes IgG1, IgG3, and IgG1, respectively (14). Furthermore, the differences in the V region sequences, including those of the complementarity-determining regions (CDRs) 3 of both H and L chains of the Abs, are evident (Fig. 1).…”

mentioning

confidence: 99%

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Epitope Recognition by Diverse Antibodies Suggests Conformational Convergence in an Antibody Response

Nair

Singh

Siddiqui

et al. 2002

The Journal of Immunology

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Crystal structures of distinct mAbs that recognize a common epitope of a peptide Ag have been determined and analyzed in the unbound and bound forms. These Abs display dissimilar binding site structures in the absence of the Ag. The dissimilarity is primarily expressed in the conformations of complementarity-determining region H3, which is responsible for defining the epitope specificity. Interestingly, however, the three Abs exhibit similar complementarity-determining region conformations in the Ag binding site while recognizing the common epitope, indicating that different pathways of binding are used for Ag recognition. The epitope also exhibits conformational similarity when bound to each of these Abs, although the peptide Ag was otherwise flexible. The observed conformational convergence in the epitope and the Ag binding site was facilitated by the plasticity in the nature of interactions.

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Section: Ag-ab Interactionssupporting

confidence: 91%

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confidence: 99%

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Epitope Recognition by Diverse Antibodies Suggests Conformational Convergence in an Antibody Response

Nair

Singh

Siddiqui

et al. 2002

The Journal of Immunology

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“…X-ray analysis is probably the most precise method for the characterization of an epitope structure. However, this method is time consuming and therefore may not be preferable for epitope mapping studies (16). Other rather time consuming approaches are random phage epitope library screening and sitedirected mutagenesis (14,15,35).…”

Section: Discussionmentioning

confidence: 99%

“…Random phage epitope library screening was used for the identification of peptide sequences, which were capable of interacting with anti-HIV-gp120 Abs (14,15). X-ray analysis was used successfully for the elucidation of epitopes (16). However, this method is time consuming, because of difficulties associated with protein crystallization.…”

Section: Mass Spectrometric Characterization Of a Discontinuousmentioning

confidence: 99%

Mass Spectrometric Characterization of a Discontinuous Epitope of the HIV Envelope Protein HIV-gp120 Recognized by the Human Monoclonal Antibody 1331A

Hochleitner

Górny

Zolla‐Pazner

et al. 2000

The Journal of Immunology

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The characterization of a discontinuous epitope in the C5 region of the HIV envelope protein HIV-gp120, recognized by 1331A, a human mAb, is reported. Regions involved in affinity binding in the HIV-gp120 molecule were identified by epitope excision/extraction methods followed by matrix assisted laser desorption-time of flight mass spectrometry. In epitope excision, the protein is bound in its native conformation to an immobilized Ab and then digested with proteolytic enzymes. In epitope extraction, the protein is first digested and subsequently allowed to react with the Ab. A series of proteolytic digestions of the 1331A/HIV-gp120 complex allowed the identification of protected amino acids in two noncontinuous regions of the C5 region of HIV-gp120. Interaction of the Ab with amino acids I487 and E507 of HIV-gp120 is essential for efficient binding. This is the first application of this approach for the identification and characterization of a discontinuous epitope. The results are consistent with molecular modeling results, indicating that these amino acids are located on opposite sides of a hydrophobic pocket. This pocket is thought to be of importance for the interaction of HIV-gp120 with the transmembrane protein HIV-gp41.

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Refined structures of Bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment

Chacko¹,

Silverton²,

Smith‐Gill

et al. 1996

Proteins

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The HyHEL-5 antibody has more than a thousandfold lower affinity for bobwhite quail lysozyme (BWQL) than for hen egg-white lysozyme (HEL). Four sequence differences exist between BWQL and HEL, of which only one is involved in the interface with the Fab. The structure of bobwhite quail lysozyme has been determined in the uncomplexed state in two different crystal forms and in the complexed state with HyHEL-5, an antihen egg-white lysozyme Fab. Similar backbone conformations are observed in the three molecules of the two crystal forms of uncomplexed BWQL, although they show considerable variability in side-chain conformation. A relatively mobile segment in uncomplexed BWQL is observed to be part of the HyHEL-5 epitope. No major backbone conformational differences are observed in the lysozyme upon complex formation, but side-chain conformational differences are seen in surface residues that are involved in the interface with the antibody. The hydrogen bonding in the interface between BWQL and HyHEL-5 is similar to that in previously determined lysozyme-HyHEL-5 complexes.

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Interactions of protein antigens with antibodies.

Abstract: There are now several crystal structures of antibody Fab fragments complexed to their protein antigens. These include Fab complexes with lysozyme, two Fab complexes with influenza virus neuraminidase, and three Fab complexes with their anti-idiotype Fabs.

Cited by 512 publications

References 62 publications

Epitope Recognition by Diverse Antibodies Suggests Conformational Convergence in an Antibody Response

Epitope Recognition by Diverse Antibodies Suggests Conformational Convergence in an Antibody Response

Mass Spectrometric Characterization of a Discontinuous Epitope of the HIV Envelope Protein HIV-gp120 Recognized by the Human Monoclonal Antibody 1331A

Refined structures of Bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment

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