Abstract
The influenza virus type A (IVA) is an important pathogen which is able to cause annual epidemics and even pandemics. This fact is the consequence of the antigenic shifts and drifts capabilities of IVA, caused by the high mutation rate and the reassortment capabilities of the virus. The hemagglutinin (HA) protein constitutes the main IVA antigen and has a crucial role in the infection mechanism, being responsible for the recognition of host-specific sialic acid derivatives. Despite the relative abundance of HA sequence and serological studies, comparative structure-based analysis of HA are less investigated. The 3DFlu database contains well annotated HA representatives: 1192 models and 263 crystallographic structures. The relations between these proteins are defined using different metrics and are visualized as a network in the provided web interface. Moreover structural and sequence comparison of the proteins can be explored. Metadata information (e.g. protein identifier, IVA strain, year and location of infection) can enhance the exploration of the presented data. With our database researchers gain a useful tool for the exploration of high quality HA models, viewing and comparing changes in the HA viral subtypes at several information levels (sequence, structure, ESP). The complete and integrated view of those relations might be useful to determine the efficiency of transmission, pathogenicity and for the investigation of evolutionary tendencies of the influenza virus.Database URL: http://nucleus3d.cent.uw.edu.pl/influenza
Highlights
The influenza virus type A (IVA) is one of the most important, untamed pathogens, which can overcome the immunological control of a host and escape the pharmaceutical treatment with specific drugs [1]
The virus is responsible for recurrent epidemics causing hundreds of thousands of fatal cases annually [2]
The HA regulates the influenza virus entry into the host cell, it has a strong impact on both pathogenicity and epidemiological consequences of the IVA infection
Summary
The influenza virus type A (IVA) is one of the most important, untamed pathogens, which can overcome the immunological control of a host and escape the pharmaceutical treatment with specific drugs [1]. The specific sequence and structural features of the binding site of a given HA protein are responsible for the differential recognition of host-specific sialic acid derivatives [3, 4]. The 3DFlu database contains a collection of HA homology models, which represent the receptor binding site variability of this protein across the most common influenza strains. Another criterion for selecting this specific set of serotypes was the availability of multiple crystallographic structures.
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