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Modulation of respiratory syncytial virus-induced prostaglandin E2 production by n−3 long-chain polyunsaturated fatty acids in human respiratory epithelium

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Lipids

Abstract

Infection with respiratory syncytial virus (RSV) results in substantial infant morbidity and has been associated with the subsequent development of childhood asthma. Inflammatory mediators produced by both the epithelium and tissue leukocytes during RSV infection stimulate the release of chemotactic factors by the respiratory epithelium and the subsequent influx of inflammatory cells, predominantly neutrophils. We investigated the production of inflammatory mediators [prostaglandin E2 (PGE2), interleukin (IL)-1β, tumor necrosis factor α] and chemokines [IL-8, RANTES (regulation on activation, normal T cell expressed and secreted)] by alveolar epithelial cells in response to RSV infection. Infection of a human alveolar epithelial transformed cell line (A549 cells) with live RSV substantially increased production of PGE2, IL-8, and RANTES. By altering cell membrane FA through incorporation of the long-chain PUFA (LCPUFA) arachidonic acid, EPA, and DHA, we were subsequently able to significantly modulate PGE2 production by the infected epithelium. Because of the dynamic nature of the effects of PGE2 on lung function, regulation of this prostaglandin during RSV infection by n−3 LCPUFA has the potential to significantly alter the disease process.

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Abbreviations

A549:

human transformed alveolar epithelial cell line

AA:

arachidonic acid

COX:

cyclooxygenase

IL:

interleukin

LCPUFA:

long-chain polyunsaturated fatty acids

MOI:

multiplicity of infection

PGE2 :

prostaglandin E2

RANTES:

regulation on activation, normal T cell expressed and secreted

RSV:

respiratory syncytial virus

Th:

T helper

TNF:

tumor necrosis factor

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Correspondence to Robert Gibson.

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Bryan, DL., Hart, P., Forsyth, K. et al. Modulation of respiratory syncytial virus-induced prostaglandin E2 production by n−3 long-chain polyunsaturated fatty acids in human respiratory epithelium. Lipids 40, 1007–1011 (2005). https://doi.org/10.1007/s11745-005-1463-4

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  • DOI: https://doi.org/10.1007/s11745-005-1463-4

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