Nucleic Acids Research, Vol 26, Issue 14 3358-3363, Copyright © 1998 by Oxford University Press
JB Domachowske, KD Dyer, AG Adams, TL Leto and HF Rosenberg
Eosinophil cationic protein (ECP) is one of two RNase A-superfamily
ribonucleases found in secretory granules of human eosinophilic leukocytes.
Although the physiologic function of eosinophils [and thus of the two
eosinophil ribonucleases, ECP and eosinophil-derived neurotoxin (EDN)]
remains controversial, we have recently shown that isolated human
eosinophils promote ribonuclease-dependent toxicity toward extracellular
virions of the single-stranded RNA virus, respiratory syncytial virus,
group B (RSV-B). We have also shown that recombinant human EDN (rhEDN) can
act alone as a ribonuclease-dependent antiviral agent. In this work, we
provide a biochemical characterization of recombinant human ECP (rhECP)
prepared in baculovirus, and demonstrate that rhECP also promotes
ribonuclease- dependent antiviral activity. The rhECP described here is N-
glycosylated, as is native ECP, and has approximately 100-fold more
ribonuclease activity than non-glycosylated rhECP prepared in bacteria. The
enzymatic activity of rhECP was sensitive to inhibition by placental
ribonuclease inhibitor (RI). Although rhECP was not as effective as rhEDN
at reducing viral infectivity (500 nM rhECP reduced infectivity of RSV-B
approximately 6 fold; 500 nM rhEDN, >50 fold), the antiviral activity
appears to be unique to the eosinophil ribonucleases; no reduction in
infectivity was promoted by bovine RNase A, by the amphibian ribonuclease,
onconase, nor by the closely-related human ribonuclease, RNase k6.
Interestingly, combinations of rhEDN and rhECP did not result in either a
synergistic or even an additive antiviral effect. Taken together, these
results suggest that that the interaction between the eosinophil
ribonucleases and the extracellular virions of RSV-B may be specific and
saturable.
ARTICLES
Eosinophil cationic protein/RNase 3 is another RNase A-family ribonuclease with direct antiviral activity
Department of Pediatrics, State University of New York Health Science Center at Syracuse, Syracuse, NY 13210, USA.
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