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Originally published online as doi:10.2353/ajpath.2009.081045 on April 6, 2009

Published online before print April 6, 2009
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(American Journal of Pathology. 2009;174:1602-1608.)
© 2009 American Society for Investigative Pathology
DOI: 10.2353/ajpath.2009.081045

Short Communications

Failure to Detect the Presence of Prions in the Uterine and Gestational Tissues from a Gravida with Creutzfeldt-Jakob Disease

Xiangzhu Xiao*{dagger}, Leticia Miravalle{ddagger}, Jue Yuan*{dagger}, John McGeehan§, Zhiqian Dong*{dagger}, Robert Wyza*, Gregory T. MacLennan*, Alan M. Golichowski, Geoff Kneale§, Nicholas King||, Qingzhong Kong*{dagger}, Salvatore Spina{ddagger}, Ruben Vidal{ddagger}, Bernardino Ghetti{ddagger}, Karen Roos||, Pierluigi Gambetti*{dagger} and Wen-Quan Zou*{dagger}

From the Department of Pathology* and the National Prion Disease Pathology Surveillance Center,{dagger} Case Western Reserve University, Cleveland, Ohio; the Departments of Pathology and Laboratory Medicine,{ddagger} Obstetrics and Gynecology, and Neurology,|| Indiana University, Indianapolis, Indiana; and the Biophysics Laboratories,§ Institute of Biomedical and Biomolecular Sciences, University of Portsmouth, Portsmouth, United Kingdom

The vertical transmission of a prion disease from infected mothers to their offspring is believed to be one of the routes for the natural spread of animal prion diseases. Supporting this notion is the observation that prion infectivity occurs in the placenta of infected ewes. Furthermore, the prion protein (PrP), both in its cellular form (PrPC) and its pathological isoform (PrPSc), has been observed at the fetal-maternal interface of scrapie-infected sheep. However, whether these features of prion infectivity also hold true for human prion diseases is currently unknown. To begin to address such an important question, we examined PrP in the uterus as well as gestational tissues, including the placenta and amniotic fluid, in a pregnant woman with sporadic Creutzfeldt-Jakob disease (CJD). Although the proteinase K (PK)-resistant prion protein, PrP27-30, was present in the brain tissues of the mother, the PrP detected in the uterus, placenta, and amniotic fluid was sensitive to PK digestion. Unlike PrPC in the brain and adjacent cerebrospinal fluid, the predominant PrP species in the reproductive and gestational tissues were N-terminally truncated, similar to urine PrP. Our study did not detect abnormal PrP in the reproductive and gestational tissues in this case of CJD. Nevertheless, examination by a highly sensitive bioassay is ongoing to ascertain possible prion infectivity from CJD in the amniotic fluid.






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