#METABOLOMICS WORKBENCH huangsxtcm_20230810_063020 DATATRACK_ID:4214 STUDY_ID:ST002848 ANALYSIS_ID:AN004666 PROJECT_ID:PR001783
VERSION             	1
CREATED_ON             	September 6, 2023, 5:47 pm
#PROJECT
PR:PROJECT_TITLE                 	Lipidomes for linked CD1 proteins
PR:PROJECT_SUMMARY               	The cellular CD1 system binds lipid antigens for display to T cells. Here we
PR:PROJECT_SUMMARY               	developed a lipidomics platform that detected > 2000 distinct lipids in cellular
PR:PROJECT_SUMMARY               	CD1 complexes, demonstrating broad display of self-sphingolipids and
PR:PROJECT_SUMMARY               	phospholipids to T cells. The four types of human CD1 antigen presenting
PR:PROJECT_SUMMARY               	molecules show differing lipid capture motifs based on the length and chemical
PR:PROJECT_SUMMARY               	structures of lipids bound, pointing to general self-lipid capture mechanisms.
PR:PROJECT_SUMMARY               	For CD1a and CD1d, lipid size matches CD1 cleft volume, whereas CD1b shows
PR:PROJECT_SUMMARY               	nearly universally size mismatch with its ligands, which results from uniform
PR:PROJECT_SUMMARY               	seating of two small lipids within its large cleft. Further, the list of
PR:PROJECT_SUMMARY               	compounds that comprise the assembled CD1 lipidomes provide a resource for
PR:PROJECT_SUMMARY               	matching to bioactive lipids from other fields of research and supports the
PR:PROJECT_SUMMARY               	ongoing discovery of lipid blockers and antigens for T cells.
PR:INSTITUTE                     	Brigham and Women's Hospital
PR:LAST_NAME                     	Huang
PR:FIRST_NAME                    	Shouxiong
PR:ADDRESS                       	251 Kettering Laboratory Complex, 160 Panzeca Way, Cincinnati, OH
PR:EMAIL                         	shouxiong.huang@uc.edu
PR:PHONE                         	5135587572
#STUDY
ST:STUDY_TITLE                   	Lipidomes for linked CD1 proteins
ST:STUDY_SUMMARY                 	The cellular CD1 system binds lipid antigens for display to T cells. Here we
ST:STUDY_SUMMARY                 	developed a lipidomics platform that detected > 2000 distinct lipids in cellular
ST:STUDY_SUMMARY                 	CD1 complexes, demonstrating a broad display of self-sphingolipids and
ST:STUDY_SUMMARY                 	phospholipids to T cells. The four types of human CD1 antigen-presenting
ST:STUDY_SUMMARY                 	molecules show differing lipid capture motifs based on the length and chemical
ST:STUDY_SUMMARY                 	structures of lipids bound, pointing to general self-lipid capture mechanisms.
ST:STUDY_SUMMARY                 	For CD1a and CD1d, lipid size matches CD1 cleft volume, whereas CD1b shows a
ST:STUDY_SUMMARY                 	nearly universal size mismatch with its ligands, which results from the uniform
ST:STUDY_SUMMARY                 	seating of two small lipids within its large cleft. Further, the list of
ST:STUDY_SUMMARY                 	compounds that comprise the assembled CD1 lipidomes provides a resource for
ST:STUDY_SUMMARY                 	matching to bioactive lipids from other fields of research and supports the
ST:STUDY_SUMMARY                 	ongoing discovery of lipid blockers and antigens for T cells.
ST:INSTITUTE                     	Brigham and Women's Hospital
ST:LAST_NAME                     	Huang
ST:FIRST_NAME                    	Shouxiong
ST:ADDRESS                       	251 Kettering Laboratory Complex, 160 Panzeca Way, Cincinnati, OH
ST:EMAIL                         	shouxiong.huang@uc.edu
ST:PHONE                         	5135587572
#SUBJECT
SU:SUBJECT_TYPE                  	Cultured cells
SU:SUBJECT_SPECIES               	Homo sapiens
SU:TAXONOMY_ID                   	9606
#SUBJECT_SAMPLE_FACTORS:         	SUBJECT(optional)[tab]SAMPLE[tab]FACTORS(NAME:VALUE pairs separated by |)[tab]Raw file names and additional sample data
SUBJECT_SAMPLE_FACTORS           	Buffer-1	Buffer-1	Experimental factors:Buffer control	RAW_FILE_NAME=072712SX03_NP0725121.mzdata
SUBJECT_SAMPLE_FACTORS           	Buffer-2	Buffer-2	Experimental factors:Buffer control	RAW_FILE_NAME=072712SX04_NP0725122.mzdata
SUBJECT_SAMPLE_FACTORS           	Buffer-3	Buffer-3	Experimental factors:Buffer control	RAW_FILE_NAME=072712SX05_NP0725123.mzdata
SUBJECT_SAMPLE_FACTORS           	K562CD1a-1	K562CD1a-1	Experimental factors:CD1a	RAW_FILE_NAME=072712SX06_K562CD1a061112-0725121.mzdata
SUBJECT_SAMPLE_FACTORS           	K562CD1a-2	K562CD1a-2	Experimental factors:CD1a	RAW_FILE_NAME=072712SX07_K562CD1a061112-0725122.mzdata
SUBJECT_SAMPLE_FACTORS           	K562CD1a-3	K562CD1a-3	Experimental factors:CD1a	RAW_FILE_NAME=072712SX08_K562CD1a061112-0725123.mzdata
SUBJECT_SAMPLE_FACTORS           	K562CD1b-1	K562CD1b-1	Experimental factors:CD1b	RAW_FILE_NAME=072712SX09_K562CD1b042012-0725121.mzdata
SUBJECT_SAMPLE_FACTORS           	K562CD1b-2	K562CD1b-2	Experimental factors:CD1b	RAW_FILE_NAME=072712SX10_K562CD1b042012-0725122.mzdata
SUBJECT_SAMPLE_FACTORS           	K562CD1b-3	K562CD1b-3	Experimental factors:CD1b	RAW_FILE_NAME=072712SX11_K562CD1b042012-0725123.mzdata
SUBJECT_SAMPLE_FACTORS           	K562CD1c-1	K562CD1c-1	Experimental factors:CD1c	RAW_FILE_NAME=072712SX13_K562CD1c070112-0725121.mzdata
SUBJECT_SAMPLE_FACTORS           	K562CD1c-2	K562CD1c-2	Experimental factors:CD1c	RAW_FILE_NAME=072712SX14_K562CD1c070112-0725122.mzdata
SUBJECT_SAMPLE_FACTORS           	K562CD1c-3	K562CD1c-3	Experimental factors:CD1c	RAW_FILE_NAME=072712SX15_K562CD1c070112-0725123.mzdata
SUBJECT_SAMPLE_FACTORS           	K562CD1d-1	K562CD1d-1	Experimental factors:CD1d	RAW_FILE_NAME=072712SX16_K562CD1d072512-0725121.mzdata
SUBJECT_SAMPLE_FACTORS           	K562CD1d-2	K562CD1d-2	Experimental factors:CD1d	RAW_FILE_NAME=072712SX17_K562CD1d072512-0725122.mzdata
SUBJECT_SAMPLE_FACTORS           	K562CD1d-3	K562CD1d-3	Experimental factors:CD1d	RAW_FILE_NAME=072712SX18_K562CD1d072512-0725123.mzdata
SUBJECT_SAMPLE_FACTORS           	K562B27-1	K562B27-1	Experimental factors:B27 control	RAW_FILE_NAME=072712SX19_K562B27051612-0725121.mzdata
SUBJECT_SAMPLE_FACTORS           	K562B27-2	K562B27-2	Experimental factors:B27 control	RAW_FILE_NAME=072712SX20_K562B27051612-0725122.mzdata
SUBJECT_SAMPLE_FACTORS           	K562B27-3	K562B27-3	Experimental factors:B27 control	RAW_FILE_NAME=072712SX21_K562B27051612-0725123.mzdata
#COLLECTION
CO:COLLECTION_SUMMARY            	Lipidomic profiles were generated from lipids that were extracted from K562
CO:COLLECTION_SUMMARY            	expressed CD1a, CD1b, CD1c, and CD1d proteins compared with peptide-binding
CO:COLLECTION_SUMMARY            	protein HLA-B27 and buffer-only controls.
CO:SAMPLE_TYPE                   	Cultured cells
#TREATMENT
TR:TREATMENT_SUMMARY             	Lipidomic profiles were generated from lipids that were extracted from K562
TR:TREATMENT_SUMMARY             	expressed CD1a, CD1b, CD1c, and CD1d proteins compared with peptide-binding
TR:TREATMENT_SUMMARY             	protein HLA-B27 and buffer-only controls.
#SAMPLEPREP
SP:SAMPLEPREP_SUMMARY            	Lipid extraction. CD1 and MHC proteins were extracted in chloroform: methanol:
SP:SAMPLEPREP_SUMMARY            	water (2:2:1) (V: V: V) (Figure S1) at room temperature for 30 mins and
SP:SAMPLEPREP_SUMMARY            	centrifuged at 500g for 10 mins. The aqueous phase contained few lipids, so the
SP:SAMPLEPREP_SUMMARY            	combined interphase and organic phase were transferred and stored at -20°C for
SP:SAMPLEPREP_SUMMARY            	comparative lipidomics analysis, which was conducted in parallel with groups of
SP:SAMPLEPREP_SUMMARY            	lipid extracts. Mass spectrometry-based comparative lipidomics. Lipid eluents
SP:SAMPLEPREP_SUMMARY            	were annormalized to protein mass (20-80 μg), dried under nitrogen at 20°C,
SP:SAMPLEPREP_SUMMARY            	dissolved and briefly sonicated in starting mobile phase, which was 100% solvent
SP:SAMPLEPREP_SUMMARY            	B containing 70% hexanes, 30% isopropanol, 0.1% formic acid, and 0.05% ammonium
SP:SAMPLEPREP_SUMMARY            	hydroxide. Triplicate samples for each protein analyzed with blanks that were
SP:SAMPLEPREP_SUMMARY            	intermixed and monitored for lipid carryover, using an Agilent 1200 series HPLC
SP:SAMPLEPREP_SUMMARY            	autosampler with an Agilent 6520 Accurate-Mass Q-TOF MS controlled by MassHunter
SP:SAMPLEPREP_SUMMARY            	software. A normal phase gradient with solvent A (70% isopropanol, 30% methanol,
SP:SAMPLEPREP_SUMMARY            	0.1% formic acid, and 0.05% ammonium hydroxide) and solvent B through a
SP:SAMPLEPREP_SUMMARY            	MonoChrom Diol column (3 μm X 150 mm X 2 mm; Varian, A0542150X020) were
SP:SAMPLEPREP_SUMMARY            	connected to a MetaGuard guard column (2 mm, Varian, A0542-MG2). The binary
SP:SAMPLEPREP_SUMMARY            	gradient was monitored with solvent B with 100% at 0-10 min, 50% at 17-22 min,
SP:SAMPLEPREP_SUMMARY            	0% at 30-35 min, and 100% at 40-50 min, followed by an additional 0% for 6 min
SP:SAMPLEPREP_SUMMARY            	post-run for regeneration. Ionization occurred with a dual-electrospray
SP:SAMPLEPREP_SUMMARY            	ionization source maintained at 325°C with a drying gas flow of 5 L/min,
SP:SAMPLEPREP_SUMMARY            	nebulizer pressure of 30 pounds per square inch, and a capillary voltage of 5.5
SP:SAMPLEPREP_SUMMARY            	kV. Positive- and negative-ion modes were typically monitored between m/z
SP:SAMPLEPREP_SUMMARY            	100-3000 with the acquisition rate of 1.4 spectra/sec and 713.7 ms/spectrum.
SP:SAMPLEPREP_SUMMARY            	Internal calibrants (Agilent G1969-85001, m/z 121.050573, 922.009798) were
SP:SAMPLEPREP_SUMMARY            	continuously monitored to assess electrospray efficiency and mass accuracy.
SP:SAMPLEPREP_SUMMARY            	NanoESI-CID-MS was typically performed at a collision energy of 35V and an
SP:SAMPLEPREP_SUMMARY            	isolation width of 1.3 m/z and adjusted to optimize signal during individual
SP:SAMPLEPREP_SUMMARY            	experiments. For the semi-quantitative analysis of PCs and SMs eluted from
SP:SAMPLEPREP_SUMMARY            	cleavable CD1, the lipid eluents were normalized based on input protein and 10
SP:SAMPLEPREP_SUMMARY            	µl were injected into a reverse-phase HPLC-MS system (Agilent Poroshell EC-C18
SP:SAMPLEPREP_SUMMARY            	column, 1.9-micron, 3 x 50 mm with an Agilent 6520 QTOF mass spectrometry).(van
SP:SAMPLEPREP_SUMMARY            	't Klooster et al., 2020)
#CHROMATOGRAPHY
CH:CHROMATOGRAPHY_SUMMARY        	Triplicate samples for each protein analyzed with blanks that were intermixed
CH:CHROMATOGRAPHY_SUMMARY        	and monitored for lipid carryover, using an Agilent 1200 series HPLC autosampler
CH:CHROMATOGRAPHY_SUMMARY        	with an Agilent 6520 Accurate-Mass Q-TOF MS controlled by MassHunter software.
CH:CHROMATOGRAPHY_TYPE           	Normal phase
CH:INSTRUMENT_NAME               	Agilent 6520 Accurate-Mass Q-TOF
CH:COLUMN_NAME                   	a MonoChrom Diol column (3 μm X 150 mm X 2 mm; Varian, A0542150X020)
CH:SOLVENT_A                     	70% isopropanol, 30% methanol, 0.1% formic acid, and 0.05% ammonium hydroxide
CH:SOLVENT_B                     	70% hexanes, 30% isopropanol, 0.1% formic acid, and 0.05% ammonium hydroxide
CH:FLOW_GRADIENT                 	The binary gradient was monitored with solvent B with 100% at 0-10 min, 50% at
CH:FLOW_GRADIENT                 	17-22 min, 0% at 30-35 min, and 100% at 40-50 min, followed by an additional 0%
CH:FLOW_GRADIENT                 	for 6 min post-run for regeneration.
CH:FLOW_RATE                     	0.7 ml/min
CH:COLUMN_TEMPERATURE            	22
#ANALYSIS
AN:ANALYSIS_TYPE                 	MS
#MS
MS:INSTRUMENT_NAME               	Agilent 6520 QTOF
MS:INSTRUMENT_TYPE               	QTOF
MS:MS_TYPE                       	ESI
MS:ION_MODE                      	POSITIVE
MS:MS_COMMENTS                   	MS data were acquired with MassHunter software.
MS:MS_RESULTS_FILE               	ST002848_AN004666_Results.txt	UNITS:542	Has m/z:Yes	Has RT:Yes	RT units:Minutes
#END