SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE
Abstract. Besides the multiple hydrolytic enzymes, lysosomes are equipped with proteins apt to activate sphyngo-lipids — saposins (SAP). SAP belong to a broad and diverse family of moderate-size (~80 AA) saposin-like proteins (SAPLIP) containing specific domains with three disulfid e bonds bridging...
| Main Authors: | , |
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| Format: | Article |
| Language: | Russian |
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Sankt-Peterburg : NIIÈM imeni Pastera
2014-07-01
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| Series: | Инфекция и иммунитет |
| Subjects: | |
| Online Access: | https://www.iimmun.ru/iimm/article/view/75 |
| _version_ | 1797967865607880704 |
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| author | V. V. Yeremeev A. S. Apt |
| author_facet | V. V. Yeremeev A. S. Apt |
| author_sort | V. V. Yeremeev |
| collection | DOAJ |
| description | Abstract. Besides the multiple hydrolytic enzymes, lysosomes are equipped with proteins apt to activate sphyngo-lipids — saposins (SAP). SAP belong to a broad and diverse family of moderate-size (~80 AA) saposin-like proteins (SAPLIP) containing specific domains with three disulfid e bonds bridging six cysteine residues. The diversity of SAPLIPS is likely explained by their involvement in distinct phases of engulfed bacteria digesting. Functionally similar SAPLIP were identified in a wide range of species — from amoeba to mammals, including humans. Saposins per se form a subfamily with six members: saposins A-D and the protein GM2 which possesses activatory functions. SAP do not have enzymatic activity, are heat-stable and protease resistant. The major in vivo function of SAP is released via participation in sphyngolipid catabolism and membrane digestion. In addition, complex association of SAP with membrane bi-layer and CD1 glycolipids is essential for loading lipid antigens onto antigen-presenting CD1 molecules for subsequent activation of lipid-specific T-cells. Of particular interest is participation of SAP in cross-presentation of bacterial antigens to CD8+ T-cells. A broad spectrum of SAP and SAPLIP involvement in the reactions of innate and adaptive immunity indicates their evolutionary conserved role in host defense. |
| first_indexed | 2024-04-11T02:37:55Z |
| format | Article |
| id | doaj.art-904c3c32ac15408f98979553e39e666b |
| institution | Directory Open Access Journal |
| issn | 2220-7619 2313-7398 |
| language | Russian |
| last_indexed | 2024-04-11T02:37:55Z |
| publishDate | 2014-07-01 |
| publisher | Sankt-Peterburg : NIIÈM imeni Pastera |
| record_format | Article |
| series | Инфекция и иммунитет |
| spelling | doaj.art-904c3c32ac15408f98979553e39e666b2023-01-02T19:37:04ZrusSankt-Peterburg : NIIÈM imeni PasteraИнфекция и иммунитет2220-76192313-73982014-07-012359760210.15789/2220-7619-2012-3-597-60275SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSEV. V. Yeremeev0A. S. Apt1Центральный НИИ туберкулеза РАМН, МоскваЦентральный НИИ туберкулеза РАМН, МоскваAbstract. Besides the multiple hydrolytic enzymes, lysosomes are equipped with proteins apt to activate sphyngo-lipids — saposins (SAP). SAP belong to a broad and diverse family of moderate-size (~80 AA) saposin-like proteins (SAPLIP) containing specific domains with three disulfid e bonds bridging six cysteine residues. The diversity of SAPLIPS is likely explained by their involvement in distinct phases of engulfed bacteria digesting. Functionally similar SAPLIP were identified in a wide range of species — from amoeba to mammals, including humans. Saposins per se form a subfamily with six members: saposins A-D and the protein GM2 which possesses activatory functions. SAP do not have enzymatic activity, are heat-stable and protease resistant. The major in vivo function of SAP is released via participation in sphyngolipid catabolism and membrane digestion. In addition, complex association of SAP with membrane bi-layer and CD1 glycolipids is essential for loading lipid antigens onto antigen-presenting CD1 molecules for subsequent activation of lipid-specific T-cells. Of particular interest is participation of SAP in cross-presentation of bacterial antigens to CD8+ T-cells. A broad spectrum of SAP and SAPLIP involvement in the reactions of innate and adaptive immunity indicates their evolutionary conserved role in host defense.https://www.iimmun.ru/iimm/article/view/75saposinssaposin-like proteinsimmunity |
| spellingShingle | V. V. Yeremeev A. S. Apt SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE Инфекция и иммунитет saposins saposin-like proteins immunity |
| title | SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE |
| title_full | SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE |
| title_fullStr | SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE |
| title_full_unstemmed | SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE |
| title_short | SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE |
| title_sort | saposin like proteins in anti infectious immune response |
| topic | saposins saposin-like proteins immunity |
| url | https://www.iimmun.ru/iimm/article/view/75 |
| work_keys_str_mv | AT vvyeremeev saposinlikeproteinsinantiinfectiousimmuneresponse AT asapt saposinlikeproteinsinantiinfectiousimmuneresponse |