Ocular Surface Expression andIn VitroActivity of Antimicrobial Peptides

Huang, Ling C., Jean, Daniele, Proske, Rita, Reins, Rose and McDermott, Alison (2007) Ocular Surface Expression andIn VitroActivity of Antimicrobial Peptides. Current Eye Research, 32 (7-8). pp. 595-609. ISSN 0271-3683

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Abstract

Purpose: Human ocular surface epithelia express four antimicrobial peptides (APs): β -defensin (hBD) 1-3 and LL-37. Here the expression of additional APs (hBD 4-6, HE2β 1; histatin-1, -3; liver expressed antimicrobial peptide-1, -2; macrophage inflammatory protein (MIP)-3α, and thymosin (T)β -4) was sought and activity against common ocular pathogens studied.

Methods: AP expression was determined in human corneal and conjunctival epithelial cells (HCEC, HCjEC) by RT-PCR and in corneal sections by immunostaining. Antimicrobial assays were performed to assess peptide (hBD 1-3, LL-37, MIP-3α, and Tβ 4) activity against Pseudomonas aeruginosa (PA), Staphylococcus aureus (SA), and Staphylococcus epidermidis (SE) in the presence of NaCl or tears. Results: HCEC and HCjEC expressed MIP-3α and Tβ 4. hBD 1-3, MIP-3α, and Tβ 4 showed activity against PA. hBD-3 had potent activity against SA and SE, whereas hBD-2, MIP-3α and Tβ 4 had moderate activity and hBD-1 had none. NaCl markedly attenuated, and tears almost completely inhibited the activity of hBD 1-2 and Tβ 4, but not that of hBD-3.

Conclusions: The ocular surface epithelia additionally express MIP-3α and Tβ 4 which have moderate antimicrobial activity. The current data support a role for hBD-3 as an antimicrobial peptide in vivo, but call in to question the effectiveness of some other APs. However, further study is required to conclusively elucidate the physiological role of each AP.

Item Type:	Article
Uncontrolled Keywords:	Antimicrobial peptides, thymosin β-4, MIP-3α/CCL20, β-defensins, cathelicidin, corneal epithelium, ocular surface, Pseudomonas aeruginosa, Staphylococcus aureus
Subjects:	B500 Ophthalmics
Department:	Faculties > Health and Life Sciences > Applied Sciences
Depositing User:	Becky Skoyles
Date Deposited:	23 May 2017 15:59
Last Modified:	12 Oct 2019 17:30
URI:	http://nrl.northumbria.ac.uk/id/eprint/30819

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