Amino terminus of the SARS coronavirus protein 3a elicits strong, potentially protective humoral responses in infected patients.
The 3a protein of severe acute respiratory syndrome (SARS)-associated coronavirus is expressed and transported to the plasma membrane in tissue cells of infected patients. Its short N-terminal ectodomain was found to elicit strong humoral responses in half of the patients who had recovered from SARS. The ectodomain-specific antibodies from the convalescent-phase plasma readily recognized and induced destruction of 3a-expressing cells in the presence of the human complement system, demonstrating their potential ability to provide immune protection by recognizing and eliminating SARS coronavirus-infected cells that express the target protein. In addition, when coupled to a carrier protein, the ectodomain peptide elicited 3a-specific antibodies in mice and rabbit at high titres. These results showed that the N terminus of the 3a protein is highly immunogenic and elicits potentially protective humoral responses in infected patients. Therefore, the short extracellular domain may be a valuable immunogen in the development of a vaccine for infectious SARS.
Zhong
Xiaofen
X
Department of Chemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.
Guo
Zufeng
Z
Biotechnology Research Institute, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.|Department of Chemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.
Yang
Huanghao
H
Biotechnology Research Institute, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.|Department of Chemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.
Peng
Lisheng
L
Department of Chemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.
Xie
Yong
Y
Department of Biology, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.
Wong
Tin-Yau
TY
Princess Margaret Hospital, Hong Kong SAR, China.
Lai
Sik-To
ST
Princess Margaret Hospital, Hong Kong SAR, China.
Guo
Zhihong
Z
Biotechnology Research Institute, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.|Department of Chemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.
D000818:Animals; D000914:Antibodies, Viral; D000917:Antibody Formation / Q000187:drug effects; D000956:Antigens, Viral / Q000276:immunology*; D006801:Humans; D051379:Mice; D011817:Rabbits; D045473:Severe acute respiratory syndrome-related coronavirus / Q000737:chemistry / Q000276:immunology*; D045169:Severe Acute Respiratory Syndrome / Q000276:immunology / Q000517:prevention & control*; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000008:administration & dosage / Q000276:immunology*; D014765:Viral Vaccines / Q000008:administration & dosage / Q000276:immunology; D000086082:Viroporin Proteins
C487105:3a protein, SARS-CoV; D000914:Antibodies, Viral; D000956:Antigens, Viral; D014759:Viral Envelope Proteins; D014764:Viral Proteins; D014765:Viral Vaccines; D000086082:Viroporin Proteins