Emily E. Putnam
University of Vermont
7 Papers
Emily E. Putnam is an academic researcher from University of Vermont. The author has contributed to research in topics: Biology & Clostridium difficile. The author has an hindex of 6, co-authored 6 publications. Previous affiliations of Emily E. Putnam include Yale University.
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Papers
Antimicrobial peptide resistance mediates resilience of prominent gut commensals during inflammation
Thomas W. Cullen,Whitman B. Schofield,Natasha A. Barry,Emily E. Putnam,E. A. Rundell,M. S. Trent,Patrick H. Degnan,Carmen J. Booth,Herbert Yu,Andrew L. Goodman +9 more
TL;DR: These findings establish a mechanism that determines the stability of prominent members of a healthy microbiota during perturbation and have identified a mechanism for lipopolysaccharide (LPS) modification in the phylum Bacteroidetes that increases AMP resistance by four orders of magnitude.
B vitamin acquisition by gut commensal bacteria.
TL;DR: Vitamins may play a critical role in driving microbiome dynamics and thus provide new avenues for modification of the microbiome and a functional link between TonB-dependent outer-membrane transport and PnuTbased inner-memBRane transport of thiamine is suggested.
The Conserved Spore Coat Protein SpoVM Is Largely Dispensable in Clostridium difficile Spore Formation.
John W. Ribis,John W. Ribis,Priyanka Ravichandran,Emily E. Putnam,Keyan Pishdadian,Aimee Shen +5 more
- 25 Oct 2017
TL;DR: The requirement of the C. difficile homolog of SpoVM, a protein that is essential for spore formation in Bacillus subtilis due to its regulation of coat and cortex formation, is determined and it is shown that SpoVM is largely dispensable for C. diffusion, in contrast with B. subtILis.
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Gut Commensal Bacteroidetes Encode a Novel Class of Vitamin B12-Binding Proteins
Emily E. Putnam,Javier Abellón-Ruiz,Bryan J. Killinger,Joshua J. Rosnow,Aaron G. Wexler,Ewa Folta-Stogniew,Aaron T. Wright,B. Van Den Berg,Andrew L. Goodman +8 more
TL;DR: A new protein is identified, BtuH, which binds vitamin B12 directly via a C-terminal globular domain that has no known structural homologs, demonstrating that members of the heterogeneous suite of accessory proteins encoded in Bacteroides cobamide transport system loci can play key roles in vitamin acquisition.
Structural and Functional Analysis of the CspB Protease Required for Clostridium Spore Germination
TL;DR: This study demonstrates that CspB is a subtilisin-like serine protease whose activity is essential for efficient SleC cleavage and C. difficile spore germination, and solves the first crystal structure of a Csp family member, Csp B, to 1.6 Å, and reveals that CSp proteases contain a unique jellyroll domain insertion critical for stabilizing the protease in vitro and in C.difficile.