Acid-base titration of melanocortin peptides: evidence of Trp rotational conformer interconversion

Abstract: Tryptophan time-resolved fluorescence was used to monitor acid-base titration properties of ␣-melanocyte stimulating hormone (␣-MSH 2, 6

Boat traffic in Lampedusa waters (Strait of Sicily, Mediterranean Sea) and its relation to the coastal distribution of common bottlenose dolphin (Tursiops truncatus)

The volume of boat traffic and its potential connection to the coastal distribution of the common bottlenose dolphin (Tursiops truncatus) was evaluated off Lampedusa Island (Strait of Sicily). From July to September 2006 daily surveys were carried out at eight sites along the coast, three times a day, to assess the number, type, and size of boats moving, fishing, or stationed in Lampedusa waters. The study area was divided into four geographic areas: northwest, northeast, southwest, and southeast. Data were analyzed to determine the difference in the number of boats among the areas, sampling months, and times of day. The presence of dolphins was monitored by standardized land-based observations. Dolphins (n = 139) from 38 sightings were observed throughout the study period (90 days). In order to compare the presence of dolphins among areas, a relative abundance index was used: A-EH (number of sighted specimens per effort hour). Common bottlenose dolphins appeared to be broadly distributed around Lampedusa, although this study highlighted a possible overlap between their habitat, boat traffic, and fishery, especially in the southwest.

Characterization of the viral O-glycopeptidome:a novel tool of relevance for vaccine design and serodiagnosis

Viral envelope proteins mediate interactions with host cells, leading to internalization and intracellular propagation. Envelope proteins are glycosylated and are known to serve important functions in masking host immunity to viral glycoproteins. However, the viral infectious cycle in cells may also lead to aberrant glycosylation that may elicit immunity. Our knowledge of immunity to aberrant viral glycans and glycoproteins is limited, potentially due to technical limitations in identifying immunogenic glycans and glycopeptide epitopes. This work describes three different complementary methods for high-throughput screening and identification of potential immunodominant O-glycopeptide epitopes on viral envelope glycoproteins: (i) on-chip enzymatic glycosylation of scan peptides, (ii) chemical glycopeptide microarray synthesis, and (iii) a one-bead-one-compound random glycopeptide library. We used herpes simplex virus type 2 (HSV-2) as a model system and identified a simple O-glycopeptide pan-epitope, (501)PPA(GalNAc)TAPG(507), on the mature gG-2 glycoprotein that was broadly recognized by IgG antibodies in HSV-2-infected individuals but not in HSV-1-infected or noninfected individuals. Serum reactivity to the extended sialyl-T glycoform was tolerated, suggesting that self glycans can participate in immune responses. The methods presented provide new insight into viral immunity and new targets for immunodiagnostic and therapeutic measures

Lectin Domains of Polypeptide GalNAc Transferases Exhibit Glycopeptide Binding Specificity*

UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferases (GalNAc-Ts) constitute a family of up to 20 transferases that initiate mucin-type O-glycosylation. The transferases are structurally composed of catalytic and lectin domains. Two modes have been identified for the selection of glycosylation sites by GalNAc-Ts: confined sequence recognition by the catalytic domain alone, and concerted recognition of acceptor sites and adjacent GalNAc-glycosylated sites by the catalytic and lectin domains, respectively. Thus far, only the catalytic domain has been shown to have peptide sequence specificity, whereas the primary function of the lectin domain is to increase affinity to previously glycosylated substrates. Whether the lectin domain also has peptide sequence selectivity has remained unclear. Using a glycopeptide array with a library of synthetic and recombinant glycopeptides based on sequences of mucins MUC1, MUC2, MUC4, MUC5AC, MUC6, and MUC7 as well as a random glycopeptide bead library, we examined the binding properties of four different lectin domains. The lectin domains of GalNAc-T1, -T2, -T3, and -T4 bound different subsets of small glycopeptides. These results indicate an additional level of complexity in the initiation step of O-glycosylation by GalNAc-Ts