{"id":51591,"date":"2025-12-20T09:59:55","date_gmt":"2025-12-20T08:59:55","guid":{"rendered":"https:\/\/inmuno.es\/index.php\/2025\/12\/20\/decoding-the-cryptic-proteome-between-antigens-and-novel-functional-proteins-valueemma-g-bawden-sebastian-amigorena-yago-a-arribas\/"},"modified":"2025-12-20T09:59:55","modified_gmt":"2025-12-20T08:59:55","slug":"decoding-the-cryptic-proteome-between-antigens-and-novel-functional-proteins-valueemma-g-bawden-sebastian-amigorena-yago-a-arribas","status":"publish","type":"post","link":"https:\/\/inmuno.es\/index.php\/2025\/12\/20\/decoding-the-cryptic-proteome-between-antigens-and-novel-functional-proteins-valueemma-g-bawden-sebastian-amigorena-yago-a-arribas\/","title":{"rendered":"Decoding the Cryptic Proteome Between Antigens and Novel Functional Proteins. [[{“value”:”Emma G. Bawden, \nSebastian Amigorena, \nYago A. Arribas”}]]"},"content":{"rendered":"

\"Decoding<\/p>\n

Unannotated splicing and translation of non-canonical open reading frames generate a diverse repertoire of cryptic proteins. Most are rapidly degraded, rendering them possible MHC-I substrates. Yet, a subpopulation can adopt stable structures and impart advantageous functions. This dichotomy both expands the antigen landscape and provides a framework for protein evolution.<\/p>\n

<\/p>\n

ABSTRACT<\/h2>\n

The widespread translation of cryptic proteins derived from the non-coding genome expands the complexity of the human proteome. A vast majority of cryptic proteins are expressed at low levels, rapidly degraded and efficiently presented on class I major histocompatibility complexes (MHC-I). On the other hand, some cryptic proteins are stable and functional and may integrate into the proteome through ongoing selective pressures. Herein, we propose a model in which the translation of cryptic proteins increases the diversity of functional proteins on which evolution can act and, during this trial-and-error process, provides a valuable source of antigens for immunosurveillance.<\/p>","protected":false},"excerpt":{"rendered":"

Unannotated splicing and translation of non-canonical open reading frames generate a diverse repertoire of cryptic proteins. Most are rapidly degraded, rendering them possible MHC-I substrates. Yet, a subpopulation can adopt stable structures and impart advantageous functions. This dichotomy both expands the antigen landscape and provides a framework for protein evolution. ABSTRACT The widespread translation of … Read more<\/a><\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[112,42],"tags":[],"class_list":["post-51591","post","type-post","status-publish","format-standard","hentry","category-european-journal-of-immunology","category-publicaciones"],"_links":{"self":[{"href":"https:\/\/inmuno.es\/index.php\/wp-json\/wp\/v2\/posts\/51591","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/inmuno.es\/index.php\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/inmuno.es\/index.php\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/inmuno.es\/index.php\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/inmuno.es\/index.php\/wp-json\/wp\/v2\/comments?post=51591"}],"version-history":[{"count":0,"href":"https:\/\/inmuno.es\/index.php\/wp-json\/wp\/v2\/posts\/51591\/revisions"}],"wp:attachment":[{"href":"https:\/\/inmuno.es\/index.php\/wp-json\/wp\/v2\/media?parent=51591"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/inmuno.es\/index.php\/wp-json\/wp\/v2\/categories?post=51591"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/inmuno.es\/index.php\/wp-json\/wp\/v2\/tags?post=51591"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}