Single, Double and Quadruple Alanine Substitutions at Oligomeric Interfaces Identify Hydrophobicity as the Key Determinant of Human Neutrophil Alpha Defensin HNP1 Function

Zhao, Le; Tolbert, W. David; Ericksen, Bryan; Zhan, Changyou; Wu, Xueji; Yuan, Weirong; Li, Xu; Pazgier, Marzena; Lu, Wuyuan

doi:10.1371/journal.pone.0078937

Title: Single, Double and Quadruple Alanine Substitutions at Oligomeric Interfaces Identify Hydrophobicity as the Key Determinant of Human Neutrophil Alpha Defensin HNP1 Function

Journal Article · Wed Nov 13 00:00:00 EST 2013 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0078937· OSTI ID:1627653

Zhao, Le ^[1]; Tolbert, W. David ^[2]; Ericksen, Bryan ^[2]; Zhan, Changyou ^[2]; Wu, Xueji ^[2]; Yuan, Weirong ^[2]; Li, Xu ^[3]; Pazgier, Marzena ^[2]; Lu, Wuyuan ^[2]

Xi'an Jiaotong Univ., Shaanxi (China). School of Medicine, First Affiliated Hospital, Translational Medicine Center; Univ. of Maryland, Baltimore, MD (United States). School of Medicine, Institute of Human Virology and Department of Biochemistry and Molecular Biology
Univ. of Maryland, Baltimore, MD (United States). School of Medicine, Institute of Human Virology and Department of Biochemistry and Molecular Biology
Xi'an Jiaotong Univ., Shaanxi (China). School of Medicine, First Affiliated Hospital, Translational Medicine Center

HNP1 is a human alpha defensin that forms dimers and multimers governed by hydrophobic residues, including Tyr¹⁶, Ile²⁰, Leu²⁵, and Phe²⁸. Previously, alanine scanning mutagenesis identified each of these residues and other hydrophobic residues as important for function. Here we report further structural and functional studies of residues shown to interact with one another across oligomeric interfaces: I20A-HNP1 and L25A-HNP1, plus the double alanine mutants I20A/L25AHNP1 and Y16A/F28A-HNP1, and the quadruple alanine mutant Y16A/I20A/L25A/F28A-HNP1. We tested binding to HIV-1 gp120 and HNP1 by surface plasmon resonance, binding to HIV-1 gp41 and HNP1 by fluorescence polarization, inhibition of anthrax lethal factor, and antibacterial activity using the virtual colony count assay. Similar to the previously described single mutant W26A-HNP1, the quadruple mutant displayed the least activity in all functional assays, followed by the double mutant Y16A/F28A-HNP1. The effects of the L25A and I20A single mutations were milder than the double mutant I20A/ L25A-HNP1. Crystallographic studies confirmed the correct folding and disulfide pairing, and depicted an array of dimeric and tetrameric structures. These results indicate that side chain hydrophobicity is the critical factor that determines activity at these positions.

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Research Organization:: SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institutes of Health (NIH); National Institute of General Medical Sciences (NIGMS); National Center for Research Resources (NCRR)

Grant/Contract Number:: AC02-76SF00515; AI072732; AI061482

OSTI ID:: 1627653

Journal Information:: PLoS ONE, Vol. 8, Issue 11; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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Title: Single, Double and Quadruple Alanine Substitutions at Oligomeric Interfaces Identify Hydrophobicity as the Key Determinant of Human Neutrophil Alpha Defensin HNP1 Function

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