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CagL is a secretory protein which plays an important role in the invasion of the host by Helicobacter pylori. The present study was undertaken to investigate the role of CagL in methicillin-resistant Staphylococcus aureus (MRSA). The genomic DNA of MRSA P01109 was used as a template to amplify the sequence of CagL. Then the amplified product was cloned into plasmid pGEX-4T-1 and pET28a expression vectors. Expression and characterization of the CagL protein was performed. The sequence of CagL was cloned into two prokaryotic expression vectors, the positive clone pGEX-CagL and pET28a-CagL was constructed. The fusion protein was expressed in the form of glutathione-S-transferase (GST)-CagL and 6xHis-CagL. Western blot was used to show the GST-CagL and 6xHis-CagL have two bands. The molecular weight of the GST-CagL and 6xHis-CagL is about 45 kDa.

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