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Quantitative proteomic analysis of exosomes from HIV ‐1‐infected lymphocytic cells
Author(s) -
Li Ming,
Aliotta Jason M.,
Asara John M.,
Tucker Lynne,
Quesenberry Peter,
Lally Michelle,
Ramratnam Bharat
Publication year - 2012
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201100376
Subject(s) - microvesicles , cd38 , annexin a2 , annexin , annexin a5 , biology , proteome , chemistry , microbiology and biotechnology , biochemistry , cell , gene , microrna , stem cell , cd34
HIV‐1 infection causes profound effects both inside and outside of cells through multiple mechanisms, including those mediated by exosomes. Using the technique of stable isotope labeling by amino acids in cell culture, we compared protein expression patterns in the exosomal compartment of HIV ‐1‐infected and ‐uninfected lymphocytic H 9 cells. Of 770 proteins identified in two independent sets of exosomal samples, 14 proteins were found to be differentially expressed in the exosomal fraction of HIV ‐1‐infected cells versus ‐uninfected controls. Gene Ontology survey and DAVID analysis revealed that identified proteins were enriched for functional categories such as binding. Of these 14 proteins, three immunomodulatory molecules were reproducibly identified in both replicates and included ADP ‐ribosyl cyclase 1 ( CD 38), L‐lactate dehydrogenase B chain ( LDHB ), and A nnexin A5 ( ANXA 5). In addition to previously reported HIV ‐1 associations with CD 38 and LDHB , new interactions were identified and validated for ANXA 5, CD 38, and LDHB , which were found to bind to HIV ‐1 p24 and T at. In summary, our studies reveal that exosomes released from HIV ‐1‐infected cells are composed of a unique and quantitatively different protein signature and harbor regulatory molecules that impact the processes of cellular apoptosis ( ANXA 5 and LDHB ) and proliferation ( CD 38).