scholarly journals Identification of a Consensus DNA-Binding Site for the Arabidopsis thaliana SBP Domain Transcription Factor, AtSPL14, and Binding Kinetics by Surface Plasmon Resonance†

Biochemistry ◽  
2008 ◽  
Vol 47 (12) ◽  
pp. 3645-3653 ◽  
Author(s):  
Xinwen Liang ◽  
Tara J. Nazarenus ◽  
Julie M. Stone
Keyword(s):  
Arabidopsis Thaliana ◽  
Transcription Factor ◽  
Surface Plasmon Resonance ◽  
Dna Binding ◽  
Binding Site ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Kinetics ◽  
Dna Binding Site

scholarly journals Interaction of theEscherichia coliReplication Terminator Protein (Tus) with DNA:  A Model Derived from DNA-Binding Studies of Mutant Proteins by Surface Plasmon Resonance†

Biochemistry ◽  
2000 ◽  
Vol 39 (39) ◽  
pp. 11989-11999 ◽  
Author(s):  
Cameron Neylon ◽  
Susan E. Brown ◽  
Andrew V. Kralicek ◽  
Caroline S. Miles ◽  
Christopher A. Love ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Dna Binding ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Studies ◽  
Mutant Proteins ◽  
Dna Binding Studies

scholarly journals Binding Kinetics of Methylene Blue on Monolayer Graphene Investigated by Multiparameter Surface Plasmon Resonance

ACS Omega ◽  
2018 ◽  
Vol 3 (7) ◽  
pp. 7133-7140 ◽  
Author(s):  
Nur Selin Kaya ◽  
Anur Yadav ◽  
Michel Wehrhold ◽  
Laura Zuccaro ◽  
Kannan Balasubramanian
Keyword(s):  
Methylene Blue ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Kinetics ◽  
Monolayer Graphene ◽  
Kinetics Of

scholarly journals Surface Plasmon Resonance Reveals Direct Binding of Herpes Simplex Virus Glycoproteins gH/gL to gD and Locates a gH/gL Binding Site on gD

2019 ◽  
Vol 93 (15) ◽  
Author(s):  
Tina M. Cairns ◽  
Noah T. Ditto ◽  
Doina Atanasiu ◽  
Huan Lou ◽  
Benjamin D. Brooks ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Binding Site ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Geographical Area ◽  
Direct Interaction ◽  
Viral Envelope ◽  
Simplex Virus

ABSTRACTHerpes simplex virus (HSV) requires fusion between the viral envelope and host membrane. Four glycoproteins, gD, gH/gL, and gB, are essential for this process. To initiate fusion, gD binds its receptor and undergoes a conformational change that hypothetically leads to activation of gH/gL, which in turn triggers the fusion protein gB to undergo rearrangements leading to membrane fusion. Our model predicts that gD must interact with both its receptor and gH/gL to promote fusion. In support of this, we have shown that gD is structurally divided into two “faces”: one for the binding receptor and the other for its presumed interaction with gH/gL. However, until now, we have been unable to demonstrate a direct interaction between gD and gH/gL. Here, we used surface plasmon resonance to show that the ectodomain of gH/gL binds directly to the ectodomain of gD when (i) gD is captured by certain anti-gD monoclonal antibodies (MAbs) that are bound to a biosensor chip, (ii) gD is bound to either one of its receptors on a chip, and (iii) gD is covalently bound to the chip surface. To localize the gH/gL binding site on gD, we used multiple anti-gD MAbs from six antigenic communities and determined which ones interfered with this interaction. MAbs from three separate communities block gD-gH/gL binding, and their epitopes encircle a geographical area on gD that we propose comprises the gH/gL binding domain. Together, our results show that gH/gL interacts directly with gD, supporting a role for this step in HSV entry.IMPORTANCEHSV entry is a multistep process that requires the actions of four glycoproteins, gD, gH/gL, and gB. Our current model predicts that gD must interact with both its receptor and gH/gL to promote viral entry. Although we know a great deal about how gD binds its receptors, until now we have been unable to demonstrate a direct interaction between gD and gH/gL. Here, we used a highly sensitive surface plasmon resonance technique to clearly demonstrate that gD and gH/gL interact. Furthermore, using multiple MAbs with defined epitopes, we have delineated a domain on gD that is independent of that used for receptor binding and which likely represents the gH/gL interaction domain. Targeting this interaction to prevent fusion may enhance both therapeutic and vaccine strategies.

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