@article{fdi:010076664, title = {{F}rom genomic to {LC}-{MS}/{MS} evidence : analysis of {P}f{EMP}1 in {B}enin malaria cases}, author = {{K}amaliddin, {C}. and {R}ombaut, {D}. and {G}uillochon, {E}. and {R}oyo, {J}ade and {E}zinmegnon, {S}. and {A}gbota, {G}. and {H}uguet, {S}. and {G}uemouri, {S}ayeh and {P}eirera, {C}. and {C}oppee, {R}. and {B}roussard, {C}. and {A}lao, {J}. {M}. and {A}ubouy, {A}gn{\`e}s and {G}uillonneau, {F}. and {D}eloron, {P}hilippe and {B}ertin, {G}wladys}, editor = {}, language = {{ENG}}, abstract = {{B}ackground {P}f{EMP}1 is the major protein from parasitic origin involved in the pathophysiology of severe malaria, and {P}f{EMP}1 domain subtypes are associated with the infection outcome. {I}n addition, {P}f{EMP}1 variability is endless and current publicly available protein repositories do not reflect the high diversity of the sequences of {P}f{EMP}1 proteins. {T}he identification of {P}f{EMP}1 protein sequences expressed with samples remains challenging. {T}he aim of our study is to identify the different {P}f{EMP}1 proteins variants expressed within patient samples, and therefore identify {P}f{EMP}1 proteins domains expressed by patients presenting uncomplicated malaria or severe malaria in malaria endemic setting in {C}otonou, {B}enin. {M}ethods {W}e performed a multi-omic approach to decipher {P}f{EMP}1 expression at the patient's level in different clinical settings. {U}sing a combination of whole genome sequencing approach and {RNA} sequencing, we were able to identify new {P}f{EMP}1 sequences and created a new custom protein database. {T}his database was used for protein identification in mass spectrometry analysis. {R}esults {T}he differential expression analysis of {RNA}sequencing data shows an increased expression of the var domains transcripts {DBL} alpha 1.7, {DBL} alpha 1.1, {DBL} alpha 2 and {DBL} beta 12 in samples from patients suffering from {C}erebral {M}alaria compared to {U}ncomplicated {M}alaria. {O}ur approach allowed us to attribute {P}f{EMP}1 sequences to each sample and identify new peptides associated to {P}f{EMP}1 proteins in mass spectrometry. {C}onclusion {W}e highlighted the diversity of the {P}f{EMP}1 sequences from field sample compared to reference sequences repositories and confirmed the validity of our approach. {T}hese findings should contribute to further vaccine development strategies based on {P}f{EMP}1 proteins.}, keywords = {{BENIN} ; {COTONOU}}, booktitle = {}, journal = {{PL}o{S} {O}ne}, volume = {14}, numero = {6}, pages = {e0218012 [14 p.]}, ISSN = {1932-6203}, year = {2019}, DOI = {10.1371/journal.pone.0218012}, URL = {https://www.documentation.ird.fr/hor/fdi:010076664}, }