{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T14:30:39Z","timestamp":1787841039321,"version":"build-2784847793"},"reference-count":27,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"3","license":[{"start":{"date-parts":[[2025,1,10]],"date-time":"2025-01-10T00:00:00Z","timestamp":1736467200000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-sa\/4.0"}],"content-domain":{"domain":["lww.com","ovid.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2025,7]]},"abstract":"<jats:sec>\n                    <jats:title>Background &amp; objectives:<\/jats:title>\n                    <jats:p>\n                      Salivary gland proteins but not glycoconjugates have been previously studied in mosquito vectors of human diseases. Glycoconjugates from salivary gland-derived proteins from human-feeding tick vectors can elicit hypersensitivity reactions which may also occur with mosquito bites. Protein glycoconjugate in salivary glands of the principal arboviral vector\n                      <jats:italic toggle=\"yes\">Aedes aegypti<\/jats:italic>\n                      and the rapidly spreading malaria vector\n                      <jats:italic toggle=\"yes\">Anopheles stephensi<\/jats:italic>\n                      were investigated.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods:<\/jats:title>\n                    <jats:p>Forty different lectins in a microarray were used to analyse glycoconjugates in salivary gland proteins from both mosquito species.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results:<\/jats:title>\n                    <jats:p>Salivary gland glycoproteins of both mosquitoes possessed similar lectin-binding specificities. Lectin-binding profiles in both mosquitoes showed the significant presence of oligomannose N-linked glycans, O-linked glycans, a limited presence of glycan structures capped with terminal GalNAc, GlcNAc, \u03b2-linked Gal, \u03b1l-6 linked fucose, and no detectable sialic acids or terminal \u03b1-linked Gal in salivary gland glycoproteins.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Interpretation &amp; conclusion:<\/jats:title>\n                    <jats:p>\n                      <jats:italic toggle=\"yes\">Aedes aegypti<\/jats:italic>\n                      and\n                      <jats:italic toggle=\"yes\">An. stephensi<\/jats:italic>\n                      possess similar salivary gland protein glycoconjugates to mosquito larval tissues. They differ from arachnid ticks in lacking detectable \u03b1-gal epitopes that are responsible for red meat allergy caused by tick bites.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.4103\/jvbd.jvbd_147_24","type":"journal-article","created":{"date-parts":[[2025,1,10]],"date-time":"2025-01-10T12:02:38Z","timestamp":1736510558000},"page":"326-331","update-policy":"https:\/\/doi.org\/10.1097\/lww.0000000000001000","source":"Crossref","is-referenced-by-count":0,"title":["Lectin microarray analysis of salivary gland glycoproteins from arboviral vector Aedes aegypti and malaria vector Anopheles stephensi"],"prefix":"10.4103","volume":"62","author":[{"given":"Ranjan","family":"Ramasamy","sequence":"first","affiliation":[{"name":"IDFISH Technology, Milpitas, California, USA"},{"name":"Department of Zoology, Faculty of Science, University of Jaffna, Jaffna, Sri 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