Affiliations 

  • 1 Agro-Biotechnology Malaysia Institutes, c/o MARDI Headquarters, Serdang 43400, Selangor, Malaysia. yusmin_y@um.edu.my
  • 2 Centre for Foundation Studies in Science, University of Malaya, Kuala Lumpur 50603, Malaysia. yasmin@um.edu.my
  • 3 Department of Molecular Medicine, Faculty of Medicine, University of Malaya, Kuala Lumpur 50603, Malaysia. hanani@um.edu.my
  • 4 University of Malaya Centre for Proteomics Research (UMCPR), University of Malaya, Kuala Lumpur 50603, Malaysia. jaime_jacklyn@um.edu.my
  • 5 Plant Protection Unit, Sime Darby Sdn Bhd, Km 10, Jalan Banting Kelanang, P.O. Box 207, Banting 42100, Selangor, Malaysia. tchinchong@yahoo.com
  • 6 Plant Protection Unit, Sime Darby Sdn Bhd, Km 10, Jalan Banting Kelanang, P.O. Box 207, Banting 42100, Selangor, Malaysia. nanniiez82@gmail.com
  • 7 Department of Molecular Medicine, Faculty of Medicine, University of Malaya, Kuala Lumpur 50603, Malaysia. jaime_jacklyn@um.edu.my
  • 8 Centre for Research in Biotechnology for Agriculture, University of Malaya, Kuala Lumpur 50603, Malaysia. yasmin@um.edu.my
  • 9 Department of Molecular Medicine, Faculty of Medicine, University of Malaya, Kuala Lumpur 50603, Malaysia. onnhashim@um.edu.my
Int J Mol Sci, 2014;15(3):5175-92.
PMID: 24663087 DOI: 10.3390/ijms15035175

Abstract

Basal stem rot is a common disease that affects oil palm, causing loss of yield and finally killing the trees. The disease, caused by fungus Ganoderma boninense, devastates thousands of hectares of oil palm plantings in Southeast Asia every year. In the present study, root proteins of healthy oil palm seedlings, and those infected with G. boninense, were analyzed by 2-dimensional gel electrophoresis (2-DE). When the 2-DE profiles were analyzed for proteins, which exhibit consistent significant change of abundance upon infection with G. boninense, 21 passed our screening criteria. Subsequent analyses by mass spectrometry and database search identified caffeoyl-CoA O-methyltransferase, caffeic acid O-methyltransferase, enolase, fructokinase, cysteine synthase, malate dehydrogenase, and ATP synthase as among proteins of which abundances were markedly altered.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.