PMID- 38382459
OWN - NLM
STAT- MEDLINE
DCOM- 20240412
LR  - 20240425
IS  - 1349-7006 (Electronic)
IS  - 1347-9032 (Print)
IS  - 1347-9032 (Linking)
VI  - 115
IP  - 4
DP  - 2024 Apr
TI  - Emerging potential of immunopeptidomics by mass spectrometry in cancer 
      immunotherapy.
PG  - 1048-1059
LID - 10.1111/cas.16118 [doi]
AB  - With significant advances in analytical technologies, research in the field of 
      cancer immunotherapy, such as adoptive T cell therapy, cancer vaccine, and immune 
      checkpoint blockade (ICB), is currently gaining tremendous momentum. Since the 
      efficacy of cancer immunotherapy is recognized only by a minority of patients, 
      more potent tumor-specific antigens (TSAs, also known as neoantigens) and 
      predictive markers for treatment response are of great interest. In cancer 
      immunity, immunopeptides, presented by human leukocyte antigen (HLA) class I, 
      play a role as initiating mediators of immunogenicity. The latest advancement in 
      the interdisciplinary multiomics approach has rapidly enlightened us about the 
      identity of the "dark matter" of cancer and the associated immunopeptides. In 
      this field, mass spectrometry (MS) is a viable option to select because of the 
      naturally processed and actually presented TSA candidates in order to grasp the 
      whole picture of the immunopeptidome. In the past few years the search space has 
      been enlarged by the multiomics approach, the sensitivity of mass spectrometers 
      has been improved, and deep/machine-learning-supported peptide search algorithms 
      have taken immunopeptidomics to the next level. In this review, along with the 
      introduction of key technical advancements in immunopeptidomics, the potential 
      and further directions of immunopeptidomics will be reviewed from the perspective 
      of cancer immunotherapy.
CI  - (c) 2024 The Authors. Cancer Science published by John Wiley & Sons Australia, Ltd 
      on behalf of Japanese Cancer Association.
FAU - Minegishi, Yuriko
AU  - Minegishi Y
AUID- ORCID: 0009-0001-1655-1902
AD  - Cancer Proteomics Group, Cancer Precision Medicine Center, Japanese Foundation 
      for Cancer Research, Tokyo, Japan.
FAU - Haga, Yoshimi
AU  - Haga Y
AUID- ORCID: 0000-0001-7861-617X
AD  - Cancer Proteomics Group, Cancer Precision Medicine Center, Japanese Foundation 
      for Cancer Research, Tokyo, Japan.
FAU - Ueda, Koji
AU  - Ueda K
AUID- ORCID: 0000-0001-9066-4959
AD  - Cancer Proteomics Group, Cancer Precision Medicine Center, Japanese Foundation 
      for Cancer Research, Tokyo, Japan.
LA  - eng
GR  - 20ae0101074s0302/Japan Agency for Medical Research and Development/
GR  - Shimadzu Corporation/
GR  - 23K04971/Japan Society for the Promotion of Science/
PT  - Journal Article
PT  - Review
DEP - 20240221
PL  - England
TA  - Cancer Sci
JT  - Cancer science
JID - 101168776
RN  - 0 (Histocompatibility Antigens Class I)
RN  - 0 (Antigens, Neoplasm)
SB  - IM
MH  - Humans
MH  - *Neoplasms/therapy
MH  - Histocompatibility Antigens Class I
MH  - Antigens, Neoplasm
MH  - Mass Spectrometry/methods
MH  - Immunotherapy
PMC - PMC11007014
OTO - NOTNLM
OT  - cancer immunotherapy
OT  - immunopeptidomics
OT  - mass spectrometry
OT  - neoantigen
COIS- K.U. is an editorial board member of Cancer Science. Y.M. and Y.H. have no 
      conflicts of interest.
EDAT- 2024/02/22 00:43
MHDA- 2024/04/12 06:44
PMCR- 2024/02/21
CRDT- 2024/02/21 18:17
PHST- 2024/02/02 00:00 [revised]
PHST- 2023/12/18 00:00 [received]
PHST- 2024/02/07 00:00 [accepted]
PHST- 2024/04/12 06:44 [medline]
PHST- 2024/02/22 00:43 [pubmed]
PHST- 2024/02/21 18:17 [entrez]
PHST- 2024/02/21 00:00 [pmc-release]
AID - CAS16118 [pii]
AID - 10.1111/cas.16118 [doi]
PST - ppublish
SO  - Cancer Sci. 2024 Apr;115(4):1048-1059. doi: 10.1111/cas.16118. Epub 2024 Feb 21.