Update nhi.md

issue #248 (closed)

content/3.defense-systems/nhi.md

@@ -10,24 +10,21 @@ tableColumns:
     Activator: Direct binding
     Effector: Nucleic acid degrading
     PFAM: PF01443, PF09848, PF13604
-
 contributors:
-- Alba Herrero del Valle
-## Relevant abstracts
-
-::relevant-abstracts
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-items:
-    - doi: 10.1016/j.chom.2022.03.001
-
----
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+  - Alba Herrero del Valle
+relevantAbstracts:
+  - doi: 10.1016/j.chom.2022.03.001
+  - doi: 10.1016/j.chom.2022.09.017
 ---
 
 # Nhi
+
 ## Description
+
 The Nhi (nuclease-helicase immunity) system targets and degrades specific phage DNA replication intermediates :ref{doi=10.1016/j.chom.2022.03.001}.  Nayeemul Bari et al. showed that Nhi from *Staphylococcus epidermidis* protects against a diverse panel of staphylococcal phages and Millman et al. showed that a protein Nhi-like (that shares the domain organization with Nhi but not the sequence) from *Bacillus cereus* protects against some Bacillus phages :ref{doi=10.1016/j.chom.2022.03.001,10.1016/j.chom.2022.09.017}. 
+
 ## Molecular mechanisms
+
 Nhi contains two domains, a nuclease and a helicase domain that are both needed for the anti-phage activity. The nuclease domain has 3′–5′ exonuclease and plasmid nicking activities while the helicase unwinds dsDNA biderctionally. Nhi specifically recognizes phage single-stranded DNA binding proteins (SSB) that cover the phage genome to target this DNA for degradation thanks to its helicase and nuclease domains :ref{doi=10.1016/j.chom.2022.03.001}.
 
 ## Example of genomic structure
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