Structural Constraints for the Binding of Short Peptides to Claudin-4 Revealed by Surface Plasmon Resonance

Ling, Jun; Liao, Hailing; Clark, Robin T.; Wong, Mandy Sze Man; Lo, David

doi:10.1074/jbc.m803548200

Cited by 62 publications

(62 citation statements)

References 23 publications

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“…Indeed, substitutions of M150L/A153P in the Cld4 ECL2 peptide enabled binding to GST-CPE-(116 -319) ( Table 2). Our results with ECL2 peptides and full-length claudins, as well as other reports (38), are consistent with the idea that transmembrane segments stabilize the native conformation of the ECL2 and, thereby, increase the affinity of the CPE-claudin interaction.…”

Section: Structural Determinants Support An Interaction Of the Helixtsupporting

confidence: 80%

“…Similar results have been reported by others earlier. They found that CPE peptides do not bind to claudin-4 fragments without transmembrane segments (38). Strikingly, Cld4 and -8 do not contain the conserved second proline implicated in the stabilization of the loop structure (11).…”

Section: Structural Determinants Support An Interaction Of the Helixtmentioning

confidence: 99%

“…Others have speculated that aromatic residues in claudin could also interact with the aromatic residues in CPE (38). But interestingly, removal of the aromatic residues (F147A, Y148A, Y158A) in Cld5 resulted in an increase in binding of GST-CPE-(116 -319) to transfected cells (Fig.…”

Section: Structural Determinants Support An Interaction Of the Helixtmentioning

confidence: 99%

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Molecular Determinants of the Interaction between Clostridium perfringens Enterotoxin Fragments and Claudin-3

Winkler¹,

Gehring

Wenzel

et al. 2009

Journal of Biological Chemistry

106

144

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Section: Structural Determinants Support An Interaction Of the Helixtsupporting

confidence: 80%

Section: Structural Determinants Support An Interaction Of the Helixtmentioning

confidence: 99%

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Molecular Determinants of the Interaction between Clostridium perfringens Enterotoxin Fragments and Claudin-3

Winkler¹,

Gehring

Wenzel

et al. 2009

Journal of Biological Chemistry

106

144

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show abstract

“…Surface Plasmon Resonance-To analyze HIV-1 RT T/P interaction, we utilized a surface plasmon resonance technology that was previously described (26,27). In this study we used a Biacore T200 (Biacore Inc., Piscataway, NJ) and a Series S streptavidin-coated (SA) sensor chip (GE Healthcare).…”

Section: Methodsmentioning

confidence: 99%

Effect of Ribonucleotides Embedded in a DNA Template on HIV-1 Reverse Transcription Kinetics and Fidelity

Daddacha

Noble²,

Nguyen

et al. 2013

Journal of Biological Chemistry

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Background: Under limiting dNTP concentrations, HIV-1 RT incorporates rNTPs during DNA synthesis. Results: HIV-1 RT utilizes dNTP less efficiently around rNMPs, and mismatch extension fidelity is significantly reduced. Conclusion: Presence of an rNMP in DNA template slows HIV-1 RT-mediated DNA synthesis and reduces fidelity. Significance: This study provides insight into how rNMP incorporation during proviral DNA synthesis can affect HIV-1 replication kinetics and fidelity.

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“…32) Therefore ligands that target FaE or M cells may be useful for mucosal vaccination. In this regard, both FaE and M cells show considerable expression of cL-4, 19,33) suggesting the potential utility of cL-4-targeting in mucosal vaccination.…”

Section: Targeting the Mucosamentioning

confidence: 99%

Recent Advances in Claudin-Targeting Technology

Nagase

Doyama

Yagi

et al. 2013

Biological & Pharmaceutical Bulletin

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Most malignant tumors are derived from epithelium, and pathologic microorganisms often invade the body through the mucosal epithelium. Thus epithelial tissues are potent targets for drug delivery. The tight junction (TJ) is the intercellular seal in epithelial cell sheets. Claudins (CLs) are a family of tetratransmembrane proteins with a molecular mass of approximately 23 kDa. CLs are key structural and sealing components of TJs. CLs are often overexpressed in malignant tumors. CL-4 is highly expressed in the epithelial cells covering mucosal immune tissues. Therefore CLs may be potent targets for drug delivery, cancer therapy, and mucosal vaccination. Herein, we overview a series of our studies using the C-terminal fragment of Clostridium perfringens enterotoxin to target and bind CLs; we also discuss the efficacy of CL-targeted drug delivery.

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Structural Constraints for the Binding of Short Peptides to Claudin-4 Revealed by Surface Plasmon Resonance

Cited by 62 publications

References 23 publications

Molecular Determinants of the Interaction between Clostridium perfringens Enterotoxin Fragments and Claudin-3

Molecular Determinants of the Interaction between Clostridium perfringens Enterotoxin Fragments and Claudin-3

Effect of Ribonucleotides Embedded in a DNA Template on HIV-1 Reverse Transcription Kinetics and Fidelity

Recent Advances in Claudin-Targeting Technology

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