The identification of FERM domain protein in serum infected with Plasmodium berghei

Malaria continues to affect 500 million people worldwide every year. In this study, we compared the protein profile of uninfected and Plasmodium berghei-infected serum samples by one dimensional SDS-PAGE analysis, MALDI-TOF/TOF mass spectrometry and confirmed by semi-quantitative RT-PCR. Also the protein interacting networks were established using STRING protein⿿protein interaction analysis. We observed for the first time the upregulation of FERM domain during P. berghei infection. We predict that FRMD5 along with the other protein partners (identified by STRING analysis) are involved in the merozoites entry or protein trafficking where cell to cell interaction happens with the host erythrocyte; hence, upregulation.