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Host and Pathogen-Specific Drug Targets in COVID-19
Published in Debmalya Barh, Kenneth Lundstrom, COVID-19, 2022
Bruce D. Uhal, David Connolly, Farzaneh Darbeheshti, Yong-Hui Zheng, Ifeanyichukwu E. Eke, Yutein Chung, Lobelia Samavati
Sialic acids are a family of monosaccharides attached to various glycolipids and glycoproteins on epithelial cell membranes. That is why sialic acids are considered a highly accessible cell membrane component for receptor–ligand and protein–ligand interactions. In the context of virology, sialic acids were the first characterized receptors promoting the viral entry process [20]. Viral entry through the sialic acid-dependent manner has been shown in several types of coronaviruses based on enzymatic activities of hemagglutinin esterase [21]. Concerning SARS-CoV-2, specific sialic acids [22] on the respiratory tract’s epithelium could be employed as co-receptors for the S protein so that virus clustering is facilitated. Moreover, ACE2, as the primary receptor for SARS-CoV-2 attachment, is heavily sialylated on N- and O-linked sugar chains. Consequently, the sialic acid-mediating targeted therapies may inhibit SARS-CoV-2 invasion by inhibiting virus–host cell interaction and modulation of endocytosis. However, the host sialome could also play a protective role against viral infections by providing a large layer of sialylated residues on mucosal cell surfaces and interfering with virus entry by offering an alternative binding site. This section aims to summarize the potential sialic acid-mediating targeted therapies in COVID-19 and provides insight into their molecular mechanisms (Figure 10.1).
The Aedes Fauna: Different Aedes Species Inhabiting the Earth
Published in Jagriti Narang, Manika Khanuja, Small Bite, Big Threat, 2020
Annette Angel, Bennet Angel, Neelam Yadav, Jagriti Narang, Surender Singh Yadav, Vinod Joshi
Not much data is available on the gene sequencing of the species Aedes triseriatus, however, salivary gland proteins have been sequenced, which is important from virus transmission point of view. Like other Aedes mosquitoes, the saliva of Aedes triseriatus is highly allergic and also has vasodilating properties (Edwards et al., 1998; Peng et al., 1998; Reno and Novak, 2005; Ribeiro et al., 1994). Studies were undertaken by Calvo and team to develop a salivary repertoire or sialome that would be useful for understanding the causation of allergy and thus indirectly provide new knowledge for development of vaccines and chemotherapeutics (Calva et al., 2010). Other than this, Beck and coworkers have studied a gene known as the AtlAP1 (Aedes triseriatus inhibitor of apoptosis 1) which is responsible for the ability to vertically transmit the La Crosse virus (Beck et al., 2009). Searching the NCBI database for protein submission of the species indicates partial sequence available for proteins like COX1, putative disulfide isomerase, inhibitor of apotosis protein 1-like protein, putative chaperonin containing t-complex polypeptide 1 CCT delta subunit, putative large subunit ribosomal protein rpL44, enolase, arginine kinase-like protein, actin, argonaute 2, and vitellogenin C.
Biting insect and tick allergens
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2020
Donald R. Hoffman, Jennifer E. Fergeson
The characterization of allergens from saliva of biting insects is very limited; those studies where allergens have been identified typically show that some of the major salivary proteins are allergens. According to Ribeiro, blood feeding evolved independently multiple times among hematophagous arthropods [11]. A variety of anticlotting factors, platelet aggregation antagonists, and vasodilators developed to counter the host's hemostatic and immunomodulatory factors [12]. In addition, arthropod saliva contains digestive enzymes [13] and hyaluronidase. One unsuspected property of some insect saliva is enhancement of infectivity of parasites carried by arthropod vectors [14]. Sand fly saliva decreases the minimum effective dose of Leishmania major in mice by several orders of magnitude. In a 2012 review, Mecheri proposed that innate and specific immune responses to Anopheles salivary components are important in the pathogenesis of malaria [15]. He provides evidence for the importance of both pro-inflammatory mediators from mast cells and the antigen-specific IgE-mediated response. In 2002 the first complete genome sequence of a biting insect, the malaria mosquito, Anopheles gambiae, became available [16]. The set of proteins expressed by the salivary glands has been named the sialome by Ribeiro and are mapped for mosquitoes, kissing bugs, and ticks [17–20].
Characterization of tick salivary gland and saliva alphagalactome reveals candidate alpha-gal syndrome disease biomarkers
Published in Expert Review of Proteomics, 2021
Margarita Villar, Iván Pacheco, Lourdes Mateos-Hernández, Alejandro Cabezas-Cruz, Ala E. Tabor, Manuel Rodríguez-Valle, Albert Mulenga, Katherine M. Kocan, Edmour F. Blouin, José de La Fuente
Selected spots reactive to anti-α-Gal antibodies and/or Patient 1, Patient 2 and healthy control sera were analyzed by proteomics (Figure 4 and Table 2). As expected, all identified proteins were present in the A. americanum sialome SG (Table 2). These results validated the presence of proteins with α-Gal modifications in the tick sialome SG (Figure 4 and Table 2). Proteins reactive to anti-α-Gal antibodies in Spots 1 and 2 were also identified by sera from Patient 1 (Spots 1) and Patient 2 and Control (Spots 2). Proteins without α-Gal modifications in Spots 3 were reactive only to serum from Patient 2. Proteins in Spots 2 with α-Gal modifications and reactive to serum from healthy control individual and Patient 2 may be an indicator of exposure to tick bites and included multiple Glycine-rich secreted cement proteins and other structural proteins (Table 2). These proteins were not identified by Patient’s 1 serum, which suggests that in cases with more severe AGS symptomatology the antibody response is predominantly directed against candidate disease markers.