It is estimated that out of approximately 31.4 million people living in North-eastern India, about 8.1 million are tribal people of the hills and plains. Among four of the seven north-eastern states, tribal people are in majority. Arunachal Pradesh is made of approximately 24 major tribal groups, which constitute about 70% of the total population, Tripura 29% and in Assam constitutes 11%. A total of 1726 cases were randomly selected in this study, out of which 1263 cases were from North-east India, namely from Arunachal Pradesh, Assam, Tripura and the rest were from West Bengal. Hematological parameters were estimated and agarose gel electrophoresis for identification of the Hb variants was performed. DNA was isolated, amplified and analysed by PCR-ARMS technology. The incidence of anemia among the tribal people of Assam was 59.82%, in Arunachal Pradesh 53.77% and Tripura 57.45%. The presence of hemoglobinopathies and thalassemia account for anemia in a sizeable population of the north-eastern states in certain tribes and urgent health resources are needed to deal with this. HbE appears to be the commonest hemoglobin among the different tribes of north-east.

BackgroundPcrV is a hydrophilic translocator of type three secretion system (TTSS) and a structural component of the functional translocon. C-terminal helix of PcrV is essential for its oligomerization at the needle tip. Conformational changes within PcrV regulate the effector translocation. PcrG is a cytoplasmic regulator of TTSS and forms a high affinity complex with PcrV. C-terminal residues of PcrG control the effector secretion.ResultBoth PcrV and PcrG-PcrV complex exhibit elongated conformation like their close homologs LcrV and LcrG-LcrV complex. The homology model of PcrV depicts a dumbbell shaped structure with N and C-terminal globular domains. The grip of the dumbbell is formed by two long helices (helix-7 and 12), which show high level of conservation both structurally and evolutionary. PcrG specifically protects a region of PcrV extending from helix-12 to helix-7, and encompassing the C-terminal globular domain. This fragment ∆PcrV(128–294) interacts with PcrG with high affinity, comparable to the wild type interaction. Deletion of N-terminal globular domain leads to the oligomerization of PcrV, but PcrG restores the monomeric state of PcrV by forming a heterodimeric complex. The N-terminal globular domain (∆PcrV(1–127)) does not interact with PcrG but maintains its monomeric state. Interaction affinities of various domains of PcrV with PcrG illustrates that helix-12 is the key mediator of PcrG-PcrV interaction, supported by helix-7. Bioinformatic analysis and study with our deletion mutant ∆PcrG(13–72) revealed that the first predicted intramolecular coiled-coil domain of PcrG contains the PcrV interaction site. However, 12 N-terminal amino acids of PcrG play an indirect role in PcrG-PcrV interaction, as their deletion causes 40-fold reduction in binding affinity and changes the kinetic parameters of interaction. ∆PcrG(13–72) fits within the groove formed between the two globular domains of PcrV, through hydrophobic interaction.ConclusionPcrG interacts with PcrV through its intramolecular coiled-coil region and masks the domains responsible for oligomerization of PcrV at the needle tip. Also, PcrG could restore the monomeric state of oligomeric PcrV. Therefore, PcrG prevents the premature oligomerization of PcrV and maintains its functional state within the bacterial cytoplasm, which is a pre-requisite for formation of the functional translocon.

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