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Comment
. 2021 Feb 2;12(1):e03447-20.
doi: 10.1128/mBio.03447-20.

MMR Vaccine and COVID-19: Measles Protein Homology May Contribute to Cross-Reactivity or to Complement Activation Protection

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Comment

MMR Vaccine and COVID-19: Measles Protein Homology May Contribute to Cross-Reactivity or to Complement Activation Protection

Ekaterina Marakasova et al. mBio. .
No abstract available

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Figures

FIG 1
FIG 1
Structural characteristics of coronavirus surface glycoprotein and measles fusion glycoprotein. (A) Protein structure of coronavirus surface glycoprotein in complex with LCB1. The PDB accession no. 7JZU (12) was visualized by Chimera version 1.13.1 (13) and colored by secondary structure as follows: red, helix; purple, strand; gray, coil. (B) Protein structure of measles fusion glycoprotein (chain B). The PDB (5YXW [14]) for measles fusion glycoprotein was visualized by Chimera version 1.13.1 (13) and colored by secondary structure as follows: red, helix; purple, strand; gray, coil. (C) Aligned protein structures by Chimera version 1.13.1 (13). The coronavirus surface glycoprotein (7JZU [12]) (blue) and measles virus fusion glycoprotein chain B (5YXW [14]) (red) are shown. (D) Sequence comparison between coronavirus surface glycoprotein and measles virus fusion glycoprotein (chain B). Pairwise sequence analysis of coronavirus surface glycoprotein (NCBI accession no. YP_009724390.1) and measles fusion glycoprotein (5YXW_B) was performed by Emboss Needle version 6.6.0 (15). Abbreviations: C, coronavirus; M, measles. Full sequence identity: 93/1,393 (6.7%); # similarity: 152/1,393 (10.9%). Solvent accessibility for aligned sequences was calculated by RaptorX-Property (16) as follows: 45% exposed, 23% medium, and 30% buried for coronavirus surface glycoprotein and 41% exposed, 28% medium, and 30% buried for measles fusion glycoprotein (chain B).

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