Marcel A. Müller* , Janusz T. Paweska†, Patricia A. Leman†, Christian Drosten‡, Klaus Grywna‡, Alan Kemp†, Leo Braack§, Karen Sonnenberg¶, Matthias Niedrig*, and Robert Swanepoel†
Author affiliations: *Robert Koch-Institut, Berlin, Germany; †National Institute for Communicable Diseases, Sandringham, Republic of South Africa; ‡Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany; §Conservation International, Cape Town, Republic of South Africa; ¶EUROIMMUN AG, Lübeck, Germany;
Figure 1. Results of Western blot analysis with recombinant severe acute respiratory syndrome–associated coronavirus (SARS-CoV) nucleocapsid (N) and spike (S) protein. Shown are examples for SARS-CoV ELISA–positive (2, 17, 26, 31) and –negative (38, 321) bat serum specimens tested using full-length recombinant SARS-CoV N and a fragment of the S protein (amino acids 318–510). Serum specimens were diluted 1:2,500 (left strips) and 1:5,000 (right strips). Secondary detection was performed by incubating the nitrocellulose strips with horseradish peroxidase (HRP)–labeled goat-antibat immunoglobulin (Ig) (Bethyl, Montgomery, AL, USA) (1:10,000). For chemiluminescence, SuperSignal Dura substrate (Pierce, Rockford, IL, USA) was added and films exposed for 1 min. Serum 17* was used as a reference for comparing blots. For evaluation purposes, strips were also incubated with human SARS-CoV–positive (A, B) and –negative serum specimens C and D (HCoV-NL63 positive) at the same dilutions, using goat-antihuman Ig HRP (1:20,000) for secondary detection. Serum specimens that produced signals at a dilution of 1:5,000 were recorded as positive (+).
The opinions expressed by authors contributing to this journal do not necessarily reflect the opinions of the U.S. Department of Health and Human Services, the Public Health Service, the Centers for Disease Control and Prevention, or the authors' affiliated institutions. Use of trade names is for identification only and does not imply endorsement by any of the groups named above.