April 2009
Volume 50, Issue 13
Free
ARVO Annual Meeting Abstract  |   April 2009
Mutational Analysis of Antimicrobial Activity in Recombinant Human Lacritin
Author Affiliations & Notes
  • R. L. McKown
    Integrated Science & Technology, James Madison University, Harrisonburg, Virginia
  • E. V. Coleman
    Integrated Science & Technology, James Madison University, Harrisonburg, Virginia
  • R. W. Raab
    Integrated Science & Technology, James Madison University, Harrisonburg, Virginia
  • A. M. Deleault
    Integrated Science & Technology, James Madison University, Harrisonburg, Virginia
  • M. E. Kimberly
    Integrated Science & Technology, James Madison University, Harrisonburg, Virginia
  • G. W. Laurie
    Cell Biology, University of Virginia, Charlottesville, Virginia
  • Footnotes
    Commercial Relationships  R.L. McKown, EyeRx Research Inc., F; Office of Tech Transfer, JMU and UVA Patent Fdn, P; E.V. Coleman, None; R.W. Raab, EyeRx Research, Inc., F; Office of Tech Transfer, JMU and UVa Patent Fdn, P; A.M. Deleault, None; M.E. Kimberly, None; G.W. Laurie, EyeRx Research, Inc., C; UVa Patent Foundation and Office of Tech Transfer, JMU, P.
  • Footnotes
    Support  NIH RO1 EY013143 and NIH RO1 EY0 18222 (RLM and GWL). NIH R42 EY015376 (RLM and RWR). This research was supported by grant funding from Virginia’s Commonwealth Health Research Board (RLM)
Investigative Ophthalmology & Visual Science April 2009, Vol.50, 4264. doi:
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      R. L. McKown, E. V. Coleman, R. W. Raab, A. M. Deleault, M. E. Kimberly, G. W. Laurie; Mutational Analysis of Antimicrobial Activity in Recombinant Human Lacritin. Invest. Ophthalmol. Vis. Sci. 2009;50(13):4264.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose: : Recombinant lacritin promotes human corneal epithelial cell proliferation with a biphasic 1-10 nM dose optimum, stimulates prolonged basal tearing in rabbits, and is antimicrobial in uM concentrations. Computational analysis predicts an ordered C-terminal half with an amphipathic alpha helical region. Here we define the functional domain of antimicrobial activity in lacritin and ask if the amphipathic alpha helix is required for activity.

Methods: : Lacritin deletion mutants and site-directed point mutants were created from mature lacritin, confirmed by DNA sequencing, expressed in E. coli, and purified. Deletion variants were generated with amino acid residues removed from the ends of lacritin and selected amino acid residues in the amphipathic helix were targeted for site-directed mutagenesis. A colony forming unit assay was used to assay antimicrobial activity. Circular Dichroism conformational analysis of recombinant lacritin and mutant variants was studied using a Jasco J-810 spectroplarimeter with CD Pro Software.

Results: : The antimicrobial activity of lacritin is localized to a domain between amino acids 80 and 119 of mature lacritin; a region that encompasses the C-terminal amphipathic alpha helix. The Minimum Inhibitory Concentration (MIC) of lacritin which results in greater than 90% bacterial cell death against E. coli ranged from 0.6µM to 10µM for mature lacritin and the deletion mutants. Both gram negative and gram positive pathogenic bacteria (Staphylococcus aureus, Staphylococcus epidermidis, and Pseudomonas aeruginosa) were sensitive at physiological conditions. Individual point mutations on the hydrophobic surface of the amphipathic alpha helix altered antimicrobial activity and produced conformational changes.

Conclusions: : Recombinant lacritin is antimicrobial and bactericidal with an MIC in the uM range for gram positive and gram negative bacteria. The antimicrobial domain in lacritin is localized in the C-terminal 39 amino acids. The amphipathic alpha helix in the C-terminus of lacritin appears to play an important role in antimicrobial activity.

Keywords: lacrimal gland • cornea: tears/tear film/dry eye • cornea: epithelium 
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