Agricultural biotechnology aims to scrutinize the field crops which feed half of the world’s population by improving their agronomic traits using various biotechnological tools. Pea- an important cash crop, rich in nutrients, but frequently infected with powdery mildew (fungal disease caused by Erysiphe pisi) that destroys the whole crop and causes economic loss for growers. We, therefore, targeted this research to find the pathogen-resistant pea lines and further decipher the diversity at er locus among resistant pea lines. Screening for resistant pea lines was done with Erysiphe pisi isolates (Genebank submission: KX455922.1) under the net house and greenhouse conditions. Molecular studies revealed that the Erysiphe resistant (er1) gene was present in 40 lines out of selected 50 pea lines and the mutational character was conferred up to 36 genotypes with 11 haplotype groups. The haplotype (gene) diversity (Hd) was found to be 0.5571 ± 0.099 SD and the nucleotide diversity (Pi) was 0.0160 ± 0.0042 SD Majority of resistant lines (67%) occurred in Hap-1, other remaining haplotypes (Hap 2–10) having 33% resistant lines, each showing characteristic nucleotide substitutions with respect to reference PsMLO1 gene; genotypes from these divergent haplotypes can be used in pea resistance breeding to avoid genetic homogeneity and genetic vulnerability.

Metalloproteins are well-known for playing various physicochemical processes in all life forms, including viruses. Some life-threatening viruses (such as some members of the coronaviridae family of viruses) are emerged and remerged frequently and are rapidly transmitted throughout the globe. This study aims to identify and characterize the metal-binding proteins of the coronaviridae family of viruses and further provides insight into the metal-binding protein's role in sustaining and propagating viruses inside a host cell and in the outer environment. In the present study, the available proteome of the coronaviridae family was exploited. Identified potential metal-binding proteins were analyzed for their functional domains, structural aspects, and sub-cellular localization. We also demonstrate phylogenetic aspects of all predicted metal-binding proteins among other coronaviridae family members to understand the evolutionary trend among their respective hosts. A total of 256 proteins from 51 different species of coronaviruses are predicted as metal-binding proteins. These metal-binding proteins perform various key roles in the replication and survival of viruses within the host cell. Cysteine, aspartic acid, threonine, and glutamine are key amino acid residues interacting with respective metal ions. Our observations also indicate that the metalloproteins of this family of viruses circulated and evolved in different hosts, which supports the zoonotic nature of coronaviruses. The comprehensive information on metal-binding proteins of the coronaviridae family may be further helpful in designing novel therapeutic metalloprotein targets. Moreover, the study of viral metal-binding proteins can also help to understand the roles of metal-binding proteins in virus pathogenesis and virus-host interactions.

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