Antimicrobial Activity of Apidermin 2 from the Honeybee <i>Apis mellifera</i>
Apidermins (APDs) are known as structural cuticular proteins in insects, but their additional roles are poorly understood. In this study, we characterized the honeybee, <i>Apis mellifera</i>, APD 2 (AmAPD 2), which displays activity suggesting antimicrobial properties. In <i>A. mel...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-10-01
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| Series: | Insects |
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| Online Access: | https://www.mdpi.com/2075-4450/13/10/958 |
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| author | Bo-Yeon Kim Yun-Hui Kim Yong-Soo Choi Man-Young Lee Kwang-Sik Lee Byung-Rae Jin |
| author_facet | Bo-Yeon Kim Yun-Hui Kim Yong-Soo Choi Man-Young Lee Kwang-Sik Lee Byung-Rae Jin |
| author_sort | Bo-Yeon Kim |
| collection | DOAJ |
| description | Apidermins (APDs) are known as structural cuticular proteins in insects, but their additional roles are poorly understood. In this study, we characterized the honeybee, <i>Apis mellifera</i>, APD 2 (AmAPD 2), which displays activity suggesting antimicrobial properties. In <i>A. mellifera</i> worker bees, the <i>AmAPD 2</i> gene is transcribed in the epidermis, hypopharyngeal glands, and fat body, and induced upon microbial ingestion. Particularly in the epidermis of <i>A. mellifera</i> worker bees, the <i>AmAPD 2</i> gene showed high expression and responded strongly to microbial challenge. Using a recombinant AmAPD 2 peptide, which was produced in baculovirus-infected insect cells, we showed that AmAPD 2 is heat-stable and binds to live bacteria and fungi as well as carbohydrates of microbial cell wall molecules. This binding action ultimately induced structural damage to microbial cell walls, which resulted in microbicidal activity. These findings demonstrate the antimicrobial role of AmAPD 2 in honeybees. |
| first_indexed | 2024-03-09T20:02:30Z |
| format | Article |
| id | doaj.art-06762dd82e6e467786ad0f2ad26d101d |
| institution | Directory Open Access Journal |
| issn | 2075-4450 |
| language | English |
| last_indexed | 2024-03-09T20:02:30Z |
| publishDate | 2022-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Insects |
| spelling | doaj.art-06762dd82e6e467786ad0f2ad26d101d2023-11-24T00:38:33ZengMDPI AGInsects2075-44502022-10-01131095810.3390/insects13100958Antimicrobial Activity of Apidermin 2 from the Honeybee <i>Apis mellifera</i>Bo-Yeon Kim0Yun-Hui Kim1Yong-Soo Choi2Man-Young Lee3Kwang-Sik Lee4Byung-Rae Jin5College of Natural Resources and Life Science, Dong-A University, Busan 49315, KoreaCollege of Natural Resources and Life Science, Dong-A University, Busan 49315, KoreaDepartment of Agricultural Biology, National Academy of Agricultural Science, Wanju 55365, KoreaDepartment of Agricultural Biology, National Academy of Agricultural Science, Wanju 55365, KoreaCollege of Natural Resources and Life Science, Dong-A University, Busan 49315, KoreaCollege of Natural Resources and Life Science, Dong-A University, Busan 49315, KoreaApidermins (APDs) are known as structural cuticular proteins in insects, but their additional roles are poorly understood. In this study, we characterized the honeybee, <i>Apis mellifera</i>, APD 2 (AmAPD 2), which displays activity suggesting antimicrobial properties. In <i>A. mellifera</i> worker bees, the <i>AmAPD 2</i> gene is transcribed in the epidermis, hypopharyngeal glands, and fat body, and induced upon microbial ingestion. Particularly in the epidermis of <i>A. mellifera</i> worker bees, the <i>AmAPD 2</i> gene showed high expression and responded strongly to microbial challenge. Using a recombinant AmAPD 2 peptide, which was produced in baculovirus-infected insect cells, we showed that AmAPD 2 is heat-stable and binds to live bacteria and fungi as well as carbohydrates of microbial cell wall molecules. This binding action ultimately induced structural damage to microbial cell walls, which resulted in microbicidal activity. These findings demonstrate the antimicrobial role of AmAPD 2 in honeybees.https://www.mdpi.com/2075-4450/13/10/958<i>Apis mellifera</i>antimicrobial activityapidermincuticular proteinhoneybee |
| spellingShingle | Bo-Yeon Kim Yun-Hui Kim Yong-Soo Choi Man-Young Lee Kwang-Sik Lee Byung-Rae Jin Antimicrobial Activity of Apidermin 2 from the Honeybee <i>Apis mellifera</i> Insects <i>Apis mellifera</i> antimicrobial activity apidermin cuticular protein honeybee |
| title | Antimicrobial Activity of Apidermin 2 from the Honeybee <i>Apis mellifera</i> |
| title_full | Antimicrobial Activity of Apidermin 2 from the Honeybee <i>Apis mellifera</i> |
| title_fullStr | Antimicrobial Activity of Apidermin 2 from the Honeybee <i>Apis mellifera</i> |
| title_full_unstemmed | Antimicrobial Activity of Apidermin 2 from the Honeybee <i>Apis mellifera</i> |
| title_short | Antimicrobial Activity of Apidermin 2 from the Honeybee <i>Apis mellifera</i> |
| title_sort | antimicrobial activity of apidermin 2 from the honeybee i apis mellifera i |
| topic | <i>Apis mellifera</i> antimicrobial activity apidermin cuticular protein honeybee |
| url | https://www.mdpi.com/2075-4450/13/10/958 |
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