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There exist certain host's factors which are directly involved for rapid viral replication causing worldwide pandemic. A total of 177 phytochemicals from <jats:italic>Ocimum sanctum<\/jats:italic> (L.)<jats:italic>, Tinospora cordifolia<\/jats:italic> (Thunb.) Miers<jats:italic>, Cinnamomum camphora<\/jats:italic> (L.) J. Presl.<jats:italic>, Allium sativum<\/jats:italic> (L.)<jats:italic>, Curcuma longa<\/jats:italic> (L.), and <jats:italic>Aloe vera<\/jats:italic> (L.) Burm. f. were evaluated for their affinity to all viral proteins of H1N1. Applying drug filters and keeping the threshold of such filters relative to the standards, 82 compounds were found suitable for further analysis. Consensus scoring system was used for screening top ligands from 82 compounds, which screened the top 12 compounds. Highly conserved regions (&gt;80%) which were hydrophilic, flexible, antigenic, and also charged were screened out as potent antiviral peptides. The viral proteins were taken as the targets for the modeled peptides for protein\u2013protein docking. Further, host\u2010pathogen interacting network was constructed to unveil host factors involved in viral replication, from which unique protein clusters representing their involvement in viral reproduction were selected through mapping with pathway databases. Twelve compounds and five peptides were found to be highly effective against all the proteins of H1N1. Based on the uniqueness, 13 clusters of proteins were obtained which are engaged in cellular process, namely, viral reproduction, fructose\u20106\u2010phosphate metabolism, nitrogen compound metabolism, biosynthesis, cellular process, oligodendrocyte development, localization, multiorganism process, primary metabolism, response to unfolded protein, metabolism, and response to protein and catabolism.<\/jats:p><\/jats:sec>","DOI":"10.1002\/ddr.21475","type":"journal-article","created":{"date-parts":[[2018,10,1]],"date-time":"2018-10-01T20:20:07Z","timestamp":1538425207000},"page":"106-124","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Antiviral compound screening, peptide designing, and protein network construction of influenza a virus (strain a\/Puerto Rico\/8\/1934 H1N1)"],"prefix":"10.1002","volume":"80","author":[{"given":"Surovi","family":"Saikia","sequence":"first","affiliation":[{"name":"Chemical Sciences &amp; Technology (Natural Products Chemistry) Division CSIR North East Institute of Science &amp; Technology  Jorhat Assam India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0478-6824","authenticated-orcid":false,"given":"Manobjyoti","family":"Bordoloi","sequence":"additional","affiliation":[{"name":"Chemical Sciences &amp; Technology (Natural Products Chemistry) Division CSIR North East Institute of Science &amp; Technology  Jorhat Assam India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajeev","family":"Sarmah","sequence":"additional","affiliation":[{"name":"Allied Health Sciences Assam Down Town University  Panikhaiti, Guwahati Assam India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bhaskor","family":"Kolita","sequence":"additional","affiliation":[{"name":"Chemical Sciences &amp; Technology (Natural Products Chemistry) Division CSIR North East Institute of Science &amp; Technology  Jorhat Assam India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2018,10]]},"reference":[{"key":"e_1_2_8_1_2_1","doi-asserted-by":"publisher","DOI":"10.1080\/03602530600969374"},{"key":"e_1_2_8_1_3_1","doi-asserted-by":"crossref","first-page":"5797","DOI":"10.1128\/jvi.64.12.5797-5803.1990","article-title":"Mechanism of antigenic variation in an individual epitope on influenza virus N9 neuraminidase","volume":"64","author":"Air G. 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